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Volumn 21, Issue 31, 2014, Pages 3508-3534

Cell to cell spreading of misfolded proteins as a therapeutic target in motor neuron disease

Author keywords

Advanced glycation end products (AGEs); Amyotrophic lateral sclerosis (ALS); Autophagy; Misfolded proteins; Mitochondria; Prionoids; Renshaw cells; Stem cell therapy

Indexed keywords

ALSIN; COPPER ZINC SUPEROXIDE DISMUTASE; DYNACTIN; ESCRT PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; OPTINEURIN; PROTEIN AGGREGATE; TAR DNA BINDING PROTEIN; UNCLASSIFIED DRUG; ADVANCED GLYCATION END PRODUCT; PROTEIN;

EID: 84928660143     PISSN: 09298673     EISSN: 1875533X     Source Type: Journal    
DOI: 10.2174/0929867321666140601161534     Document Type: Article
Times cited : (15)

References (326)
  • 1
    • 0028085924 scopus 로고
    • Amyotrophic lateral sclerosis
    • Rowland, L. P. Amyotrophic lateral sclerosis. Curr. Opin. Neurol., 1994, 7(4), 310-315.
    • (1994) Curr. Opin. Neurol. , vol.7 , Issue.4 , pp. 310-315
    • Rowland, L.P.1
  • 7
    • 84878131682 scopus 로고    scopus 로고
    • TARDBP and FUS mutations associated with amyotrophic lateral sclerosis: Summary and update
    • Lattante, S.; Rouleau, G. A.; Kabashi, E. TARDBP and FUS mutations associated with amyotrophic lateral sclerosis: summary and update. Hum. Mutat., 2013, 34(6), 812-826.
    • (2013) Hum. Mutat. , vol.34 , Issue.6 , pp. 812-826
    • Lattante, S.1    Rouleau, G.A.2    Kabashi, E.3
  • 8
    • 33749554133 scopus 로고    scopus 로고
    • Characterization of amyotrophic laterasclerosis-linked P56S mutation of vesicleassociated membrane protein-associated protein B (VAPB/ALS8)
    • Kanekura K, Nishimoto I, Aiso S, Matsuoka M. Characterization of amyotrophic laterasclerosis-linked P56S mutation of vesicleassociated membrane protein-associated protein B (VAPB/ALS8). J. Biol. Chem., 2006, 281(40), 30223-30233.
    • (2006) J. Biol. Chem. , vol.281 , Issue.40 , pp. 30223-30233
    • Kanekura, K.1    Nishimoto, I.2    Aiso, S.3    Matsuoka, M.4
  • 24
    • 3943102116 scopus 로고    scopus 로고
    • Unraveling the mechanisms involved in motor neuron degeneration in ALS
    • Bruijn, L. I; Miller, T. M.; Cleveland, D. W. Unraveling the mechanisms involved in motor neuron degeneration in ALS. Annu. Rev. Neurosci., 2004, 27, 723-749.
    • (2004) Annu. Rev. Neurosci. , vol.27 , pp. 723-749
    • Bruijn, L.I.1    Miller, T.M.2    Cleveland, D.W.3
  • 25
    • 38348998584 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis: From current developments in the laboratory to clinical implications
    • Cozzolino, M.; Ferri, A.; Carrì, M. T. Amyotrophic lateral sclerosis: from current developments in the laboratory to clinical implications. Antioxid. Redox Signal., 2008, 10(3), 405-443.
    • (2008) Antioxid. Redox Signal. , vol.10 , Issue.3 , pp. 405-443
    • Cozzolino, M.1    Ferri, A.2    Carrì, M.T.3
  • 28
    • 74049164709 scopus 로고    scopus 로고
    • Non-cell autonomous toxicity in neurodegenerative disorders: ALS and beyond
    • Ilieva, H.; Polymenidou, M.; Cleveland, D. W. Non-cell autonomous toxicity in neurodegenerative disorders: ALS and beyond. J. Cell. Biol., 2009, 187(6), 761-772.
    • (2009) J. Cell. Biol. , vol.187 , Issue.6 , pp. 761-772
    • Ilieva, H.1    Polymenidou, M.2    Cleveland, D.W.3
  • 29
    • 84863845583 scopus 로고    scopus 로고
    • Transformation from a neuroprotective to a neurotoxic microglial phenotype in a mouse model of ALS
    • Liao, B.; Zhao, W.; Beers, D. R.; Henkel, J. S.; Appel, S. H. Transformation from a neuroprotective to a neurotoxic microglial phenotype in a mouse model of ALS. Exp. Neurol., 2012, 237(1), 147-152.
    • (2012) Exp. Neurol. , vol.237 , Issue.1 , pp. 147-152
    • Liao, B.1    Zhao, W.2    Beers, D.R.3    Henkel, J.S.4    Appel, S.H.5
  • 30
    • 39049126210 scopus 로고    scopus 로고
    • Protein misfolding and neurodegeneration
    • Soto, C.; Estrada, L. D. Protein misfolding and neurodegeneration. Arch. Neurol., 2008, 65, 184-189.
    • (2008) Arch. Neurol. , vol.65 , pp. 184-189
    • Soto, C.1    Estrada, L.D.2
  • 31
    • 84884683227 scopus 로고    scopus 로고
    • Cross-seeding of misfolded proteins: Implications for etiology and pathogenesis of protein misfolding diseases
    • Morales, R.; Moreno-Gonzalez, I.; Soto C. Cross-seeding of misfolded proteins: implications for etiology and pathogenesis of protein misfolding diseases. PLoS Pathog. 2013, 9(9), e1003537.
    • (2013) PLoS Pathog , vol.9 , Issue.9 , pp. e1003537
    • Morales, R.1    Moreno-Gonzalez, I.2    Soto, C.3
  • 32
    • 0038404962 scopus 로고    scopus 로고
    • Role of alpha-synuclein in 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine-induced parkinsonism in mice
    • Schlüter, O. M.; Fornai, F.; Alessandrí, M. G.; Takamori, S.; Geppert, M.; Jahn, R.; Südhof, T. C. Role of alpha-synuclein in 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine-induced parkinsonism in mice. Neuroscience, 2003, 118(4), 985-1002.
    • (2003) Neuroscience , vol.118 , Issue.4 , pp. 985-1002
    • Schlüter, O.M.1    Fornai, F.2    Alessandrí, M.G.3    Takamori, S.4    Geppert, M.5    Jahn, R.6    Südhof, T.C.7
  • 37
    • 34248192413 scopus 로고    scopus 로고
    • Mechanisms involved in the formation of dopamine-induced intracellular bodies within striatal neurons
    • Lazzeri, G.; Lenzi, P.; Busceti, C. L.; Ferrucci, M.; Falleni, A.; Bruno, V.; Paparelli, A.; Fornai, F. Mechanisms involved in the formation of dopamine-induced intracellular bodies within striatal neurons. J. Neurochem., 2007, 101(5), 1414-1427.
    • (2007) J. Neurochem. , vol.101 , Issue.5 , pp. 1414-1427
    • Lazzeri, G.1    Lenzi, P.2    Busceti, C.L.3    Ferrucci, M.4    Falleni, A.5    Bruno, V.6    Paparelli, A.7    Fornai, F.8
  • 38
    • 84864023125 scopus 로고    scopus 로고
    • Loss of spinal motor neurons and alteration of alphasynuclein immunostaining in MPTP induced Parkinsonism in mice
    • Vivacqua, G.; Biagioni, F.; Yu, S.; Casini, A.; Bucci, D.; D'Este, L.; Fornai, F. Loss of spinal motor neurons and alteration of alphasynuclein immunostaining in MPTP induced Parkinsonism in mice. J. Chem. Neuroanat., 2012, 44(2), 76-85.
    • (2012) J. Chem. Neuroanat. , vol.44 , Issue.2 , pp. 76-85
    • Vivacqua, G.1    Biagioni, F.2    Yu, S.3    Casini, A.4    Bucci, D.5    D'Este, L.6    Fornai, F.7
  • 40
    • 0035109738 scopus 로고    scopus 로고
    • Synucleinopathies: Clinical and pathological implications
    • Galvin, J. E.; Lee, V. M.; Trojanowski, J. Q. Synucleinopathies: clinical and pathological implications. Arch. Neurol., 2001, 58, 186-190.
    • (2001) Arch. Neurol. , vol.58 , pp. 186-190
    • Galvin, J.E.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 41
    • 0141725659 scopus 로고    scopus 로고
    • Neuropathological spectrum of synucleinopathies
    • Jellinger, K. A. Neuropathological spectrum of synucleinopathies. Mov. Disord. 2003, 18, S2-12.
    • (2003) Mov. Disord , vol.18 , pp. S2-S12
    • Jellinger, K.A.1
  • 42
    • 80155157847 scopus 로고    scopus 로고
    • The seeds of neurodegeneration: Prion-like spreading in ALS
    • Polymenidou, M.; Cleveland, D. W. The seeds of neurodegeneration: prion-like spreading in ALS. Cell., 2011, 147, 498-508.
    • (2011) Cell. , vol.147 , pp. 498-508
    • Polymenidou, M.1    Cleveland, D.W.2
  • 43
    • 84862780458 scopus 로고    scopus 로고
    • Advanced glycation end products and neurodegenerative diseases: Mechanisms and perspective
    • Li, J,; Liu, D.; Sun, L.; Lu, Y.; Zhang, Z. Advanced glycation end products and neurodegenerative diseases: mechanisms and perspective. J. Neurol. Sci., 2012, 317, 1-5.
    • (2012) J. Neurol. Sci. , vol.317 , pp. 1-5
    • Li, J.1    Liu, D.2    Sun, L.3    Lu, Y.4    Zhang, Z.5
  • 44
    • 84875014167 scopus 로고    scopus 로고
    • Histochemical approaches to assess cell-to-cell transmission of misfolded proteins in neurodegenerative diseases
    • Natale, G.; Pompili, E.; Biagioni, F.; Paparelli, S.; Lenzi, P.; Fornai, F. Histochemical approaches to assess cell-to-cell transmission of misfolded proteins in neurodegenerative diseases. Eur. J. Histochem., 2013, 57(1), e5.
    • (2013) Eur. J. Histochem. , vol.57 , Issue.1 , pp. e5
    • Natale, G.1    Pompili, E.2    Biagioni, F.3    Paparelli, S.4    Lenzi, P.5    Fornai, F.6
  • 45
    • 27644484061 scopus 로고    scopus 로고
    • Autophagy: Molecular machinery for self-eating
    • Yorimitsu, T.; Klionsky, D. J. Autophagy: molecular machinery for self-eating. Cell Death Differ. 2005, 12 Suppl 2, 1542-1552.
    • (2005) Cell Death Differ , vol.12 , pp. 1542-1552
    • Yorimitsu, T.1    Klionsky, D.J.2
  • 46
    • 84862295360 scopus 로고    scopus 로고
    • Apr.
    • Klionsky, D. J.; Abdalla, F. C.; Abeliovich, H.; Abraham, R. T.; Acevedo-Arozena, A.; Adeli, K.; Agholme, L.; Agnello, M.; Agostinis, P.; Aguirre-Ghiso, J. A.; Ahn, H. J.; Ait-Mohamed, O.; Ait-Si-Ali, S.; Akematsu, T.; Akira, S.; Al-Younes, H. M.;, Al-Zeer, M. A.; Albert, M. L.; Albin, R. L.; Alegre-Abarrategui, J.; Aleo, M. F.; Alirezaei, M.; Almasan, A.; Almonte-Becerril, M.; Amano, A.; Amaravadi, R.; Amarnath, S.; Amer, A. O.; Andrieu-Abadie, N.; Anantharam, V.; Ann, D. K.; Anoopkumar-Dukie, S.; Aoki, H.; Apostolova, N.; Arancia, G.; Aris, J. P.; Asanuma, K.; Asare, N. Y.; Ashida, H.; Askanas, V.; Askew, D. S.; Auberger, P.; Baba, M.; Backues, S. K.; Baehrecke, E. H.; Bahr, B. A.; Bai, X. Y.; Bailly, Y.; Baiocchi, R.; Baldini, G.; Balduini, W.; Ballabio, A.; Bamber, B. A.; Bampton, E. T.; Bánhegyi, G.; Bartholomew, C. R.; Bassham, D. C.; Bast, R. C. Jr.; Batoko, H.; Bay, B. H.; Beau, I.; Béchet, D. M.; Begley, T. J.; Behl, C.; Behrends, C.; Bekri, S.; Bellaire, B.; Bendall, L. J.; Benetti, L.; Berliocchi, L.; Bernardi, H.; Bernassola, F.; Besteiro, S.; Bhatia-Kissova, I.; Bi, X.; Biard-Piechaczyk, M.; Blum, J. S.; Boise, L. H.; Bonaldo, P.; Boone, D. L.; Bornhauser, B. C.; Bortoluci, K. R.; Bossis, I.; Bost, F.; Bourquin, J. P.; Boya, P.; Boyer-Guittaut, M.; Bozhkov, P. V.; Brady, N. R.; Brancolini, C.; Brech, A.; Brenman, J. E.; Brennand, A.; Bresnick, E. H.; Brest, P.; Bridges, D.; Bristol, M. L.; Brookes, P. S.; Brown, E. J.; Brumell, J. H.; Brunetti-Pierri, N.; Brunk, U. T.; Bulman, D. E.; Bultman, S. J,.; Bultynck, G.; Burbulla, L. F.; Bursch, W.; Butchar, J. P.; Buzgariu, W.; Bydlowski, S. P.; Cadwell, K.; Cahová, M.; Cai, D.; Cai, J.; Cai, Q.; Calabretta, B.; Calvo-Garrido, J.; Camougrand, N.; Campanella, M.; Campos-Salinas, J.; Candi, E.; Cao, L.; Caplan, A. B.; Carding, S. R.; Cardoso, S. M.; Carew, J. S.; Carlin, C. R.; Carmignac, V.; Carneiro, L. A.; Carra, S.; Caruso, R. A.; Casari, G.; Casas, C.; Castino, R.; Cebollero, E.; Cecconi, F.; Celli, J; Chaachouay, H.; Chae, H. J; Chai, C. Y.; Chan, D. C.; Chan, E. Y.; Chang, R. C.; Che, C. M.; Chen, C. C.; Chen G. C.; Chen, G. Q.; Chen, M.; Chen, Q.; Chen, S. S.; Chen, W.; Chen, X.; Chen, X.; Chen, X.; Chen, Y. G.; Chen, Y.; Chen, Y.; Chen, Y. J.; Chen, Z.; Cheng, A.; Cheng, C. H.; Cheng, Y.; Cheong, H.; Cheong, J. H.; Cherry, S.; Chess-Williams, R.; Cheung, Z. H.; Chevet, E.; Chiang, H. L.; Chiarelli, R.; Chiba, T.; Chin, L. S.; Chiou, S. H.; Chisari, F. V.; Cho, C. H.; Cho, D. H.; Choi, A. M.; Choi, D.; Choi, K. S.; Choi, M. E.; Chouaib, S.; Choubey, D.; Choubey, V.; Chu, C. T.; Chuang, T. H.; Chueh, S. H.; Chun, T.; Chwae, Y. J.; Chye, M. L.; Ciarcia, R.; Ciriolo, M. R.; Clague, M. J.; Clark, R. S.; Clarke, P. G.; Clarke, R.; Codogno, P.; Coller, H. A.; Colombo, M. I.; Comincini, S.; Condello, M.; Condorelli, F.; Cookson, M. R.; Coombs, G. H.; Coppens, I.; Corbalan, R.; Cossart, P.; Costelli, P.; Costes, S.; Coto-Montes, A.; Couve, E.; Coxon, F. P.; Cregg, J. M.; Crespo, J. L.; Cronjé, M. J.; Cuervo, A. M.; Cullen, J. J.; Czaja, M. J.; D'Amelio, M.; Darfeuille-Michaud, A.; Davids, L. M.; Davies, F. E.; De Felici, M.; De Groot, J. F.; De Haan, C. A.; De Martino, L.; De Milito, A.; De Tata, V.; Debnath, J.; Degterev, A.; Dehay, B.; Delbridge, L. M.; Demarchi, F.; Deng, Y. Z.; Dengjel, J.; Dent, P.; Denton, D.; Deretic, V.; Desai, S. D.; Devenish, R. J.; Di Gioacchino, M.; Di Paolo, G.; Di Pietro, C.; Díaz-Araya, G.; Díaz-Laviada, I.; Diaz-Meco, M. T.; Diaz-Nido, J.; Dikic, I.; Dinesh-Kumar, S. P.; Ding, W. X.; Distelhorst, C. W.; Diwan, A.; Djavaheri-Mergny, M.; Dokudovskaya, S.; Dong, Z.; Dorsey, F. C.; Dosenko, V.; Dowling, J. J.; Doxsey, S.; Dreux, M.; Drew, M. E.; Duan, Q.; Duchosal, M. A.; Duff, K.; Dugail, I.; Durbeej, M.; Duszenko, M.; Edelstein, C. L.; Edinger, A. L.; Egea, G.; Eichinger, L.; Eissa, N. T.; Ekmekcioglu, S.; El-Deiry, W. S.; Elazar, Z.; Elgendy, M.; Ellerby, L. M.; Eng, K. E.; Engelbrecht, A. M.; Engelender, S.; Erenpreisa, J.; Escalante, R.; Esclatine, A.; Eskelinen, E. L.; Espert, L.; Espina, V.; Fan, H.; Fan, J.; Fan, Q. W.; Fan, Z.; Fang, S.; Fang, Y.; Fanto, M.; Fanzani, A.; Farkas, T.; Farré, J. C.; Faure, M.; Fechheimer, M.; Feng, C. G.; Feng, J.; Feng, Q.; Feng, Y.; Fésüs, L.; Feuer, R.; Figueiredo-Pereira, M. E.; Fimia, G. M.; Fingar, D. C.; Finkbeiner, S.; Finkel, T.; Finley, K. D.; Fiorito, F.; Fisher, E. A.; Fisher, P. B.; Flajolet, M.; Florez-McClure, M. L.; Florio, S.; Fon, E. A.; Fornai, F.; Fortunato, F.; Fotedar, R.; Fowler, D. H.; Fox, H. S.; Franco, R.; Frankel, L. B.; Fransen, M.; Fuentes, J. M.; Fueyo, J.; Fujii, J.; Fujisaki, K.; Fujita, E.; Fukuda, M.; Furukawa, R. H.; Gaestel, M.; Gailly, P.; Gajewska, M.; Galliot, B.; Galy, V.; Ganesh, S.; Ganetzky, B.; Ganley, I. G.; Gao, F. B.; Gao, G. F.; Gao, J.; Garcia, L.; Garcia-Manero, G.; Garcia-Marcos, M.; Garmyn, M.; Gartel, A. L.; Gatti, E.; Gautel, M.; Gawriluk, T. R.; Gegg, M. E.; Geng, J.; Germain, M.; Gestwicki, J. E.; Gewirtz, D. A.; Ghavami, S.; Ghosh, P.; Giammarioli, A. M.; Giatromanolaki, A. N.; Gibson, S. B.; Gilkerson, R. W.; Ginger, M. L.; Ginsberg, H. N.; Golab, J.; Goligorsky, M. S.; Golstein, P.; Gomez-Manzano, C.; Goncu, E.; Gongora, C.; Gonzalez, C. D.; Gonzalez, R.; González-Estévez, C.; González-Polo, R. A.; Gonzalez-Rey, E.; Gorbunov, N. V.; Gorski, S.; Goruppi, S.; Gottlieb, R. A.; Gozuacik, D.; Granato, G. E.; Grant, G. D.; Green, K. N.; Gregorc, A.; Gros, F.; Grose, C.; Grunt, T. W.; Gual, P.; Guan, J. L.; Guan, K. L.; Guichard, S. M.; Gukovskaya, A. S.; Gukovsky, I.; Gunst, J.; Gustafsson, A. B.; Halayko, A. J.; Hale, A. N.; Halonen, S. K.; Hamasaki, M.; Han, F.; Han, T.; Hancock, M. K.; Hansen, M.; Harada, H.; Harada, M.; Hardt, S. E.; Harper, J. W.; Harris, A. L.; Harris, J.; Harris, S. D.; Hashimoto, M.; Haspel, J. A.; Hayashi, S.; Hazelhurst, L. A.; He, C.; He, Y. W.; Hébert, M. J.; Heidenreich, K. A.; Helfrich, M. H.; Helgason, G. V.; Henske, E. P.; Herman, B.; Herman, P. K.; Hetz, C.; Hilfiker, S.; Hill, J. A.; Hocking, L. J.; Hofman, P.; Hofmann, T. G.; Höhfeld, J.; Holyoake, T. L.; Hong, M. H.; Hood, D. A.; Hotamisligil, G. S.; Houwerzijl, E. J.; Høyer-Hansen, M.; Hu, B.; Hu, C. A.; Hu, H. M.; Hua, Y.; Huang, C.; Huang, J.; Huang, S.; Huang, W. P.; Huber, T. B.; Huh, W. K.; Hung, T. H.; Hupp, T. R.; Hur, G. M.; Hurley, J. B.; Hussain, S. N.; Hussey, P. J.; Hwang, J. J.; Hwang, S.; Ichihara, A.; Ilkhanizadeh, S.; Inoki, K.; Into, T.; Iovane, V.; Iovanna, J. L.; Ip, N. Y.; Isaka, Y.; Ishida, H.; Isidoro, C.; Isobe, K.; Iwasaki, A.; Izquierdo, M.; Izumi, Y.; Jaakkola, P. M.; Jäättelä, M.; Jackson, G. R.; Jackson, W. T.; Janji, B.; Jendrach, M.; Jeon, J. H.; Jeung, E. B.; Jiang, H.; Jiang, H.; Jiang, J. X.; Jiang, M.; Jiang, Q.; Jiang, X.; Jiang, X.; Jiménez, A.; Jin, M.; Jin, S.; Joe, C. O.; Johansen, T.; Johnson, D. E.; Johnson, G. V.; Jones, N. L.; Joseph, B.; Joseph, S. K.; Joubert, A. M.; Juhász, G.; Juillerat-Jeanneret, L.; Jung, C. H.; Jung, Y. K.; Kaarniranta, K.; Kaasik, A.; Kabuta, T.; Kadowaki, M.; Kagedal, K.; Kamada, Y.; Kaminskyy, V. O.; Kampinga, H. H.; Kanamori, H.; Kang, C.; Kang, K. B.; Kang, K. I.; Kang, R.; Kang, Y. A.; Kanki, T.; Kanneganti, T. D.; Kanno, H.; Kanthasamy, A. G.; Kanthasamy, A.; Karantza, V.; Kaushal, G. P.; Kaushik, S.; Kawazoe, Y.; Ke, P. Y.; Kehrl, J. H.; Kelekar, A.; Kerkhoff, C.; Kessel, D. H.; Khalil, H.; Kiel, J. A.; Kiger, A. A.; Kihara, A.; Kim, D. R.; Kim, D. H.; Kim, D. H.; Kim, E. K.; Kim, H. R.; Kim, J. S.; Kim, J. H.; Kim, J. C.; Kim, J. K.; Kim, P. K.; Kim, S. W.; Kim, Y. S.; Kim, Y.; Kimchi, A.; Kimmelman, A. C.; King, J. S.; Kinsella, T. J.; Kirkin, V.; Kirshenbaum, L. A.; Kitamoto, K.; Kitazato, K.; Klein, L.; Klimecki, W. T.; Klucken, J.; Knecht, E.; Ko, B. C.; Koch, J. C.; Koga, H.; Koh, J. Y.; Koh, Y. H.; Koike, M.; Komatsu, M.; Kominami, E.; Kong, H. J.; Kong, W. J.; Korolchuk, V. I.; Kotake, Y.; Koukourakis, M. I.; Kouri Flores, J. B.; Kovács, A. L.; Kraft, C.; Krainc, D.; Krämer, H.; Kretz-Remy, C.; Krichevsky, A. M.; Kroemer, G.; Krüger, R.; Krut, O.; Ktistakis, N. T.; Kuan, C. Y.; Kucharczyk, R.; Kumar, A.; Kumar, R.; Kumar, S.; Kundu, M.; Kung, H. J.; Kurz, T.; Kwon, H. J.; La Spada, A. R.; Lafont, F.; Lamark, T.; Landry, J.; Lane, J. D.; Lapaquette, P.; Laporte, J. F.; László, L.; Lavandero, S.; Lavoie, J. N.; Layfield, R.; Lazo, P. A.; Le, W.; Le Cam, L.; Ledbetter, D. J.; Lee, A. J.; Lee, B. W.; Lee, G. M.; Lee, J.; Lee, J. H.; Lee, M.; Lee, M. S.; Lee, S. H.; Leeuwenburgh, C.; Legembre, P.; Legouis, R.; Lehmann, M.; Lei, H. Y.; Lei, Q. Y.; Leib, D. A.; Leiro, J.; Lemasters, J. J.; Lemoine, A.; Lesniak, M. S.; Lev, D.; Levenson, V. V.; Levine, B.; Levy, E.; Li, F.; Li, J. L.; Li, L.; Li, S.; Li, W.; Li, X. J.; Li, Y. B.; Li, Y. P.; Liang, C.; Liang, Q.; Liao, Y. F.; Liberski, P. P.; Lieberman, A.; Lim, H. J.; Lim, K. L.; Lim, K.; Lin, C. F.; Lin, F. C.; Lin, J.; Lin, J. D.; Lin, K.; Lin, W. W.; Lin, W. C.; Lin, Y. L.; Linden, R.; Lingor, P.; Lippincott-Schwartz, J.; Lisanti, M. P.; Liton, P. B.; Liu, B.; Liu, C. F.; Liu, K.; Liu, L.; Liu, Q. A.; Liu, W.; Liu, Y. C.; Liu, Y.; Lockshin, R. A.; Lok, C. N.; Lonial, S.; Loos, B.; Lopez-Berestein, G.; López-Otín, C.; Lossi, L.; Lotze, M. T.; Lw, P.; Lu, B.; Lu, B.; Lu, B.; Lu, Z.; Luciano, F.; Lukacs, N. W.; Lund, A. H.; Lynch-Day, M. A.; Ma, Y.; Macian, F.; MacKeigan, J. P.; Macleod, K. F.; Madeo, F.; Maiuri, L.; Maiuri, M. C.; Malagoli, D.; Malicdan, M. C.; Malorni, W.; Man, N.; Mandelkow, E. M.; Manon, S.; Manov, I.; Mao, K.; Mao, X.; Mao, Z.; Marambaud, P.; Marazziti, D.; Marcel, Y. L.; Marchbank, K.; Marchetti, P.; Marciniak, S. J.; Marcondes, M.; Mardi, M.; Marfe, G.; Mariño, G.; Markaki, M.; Marten, M. R.; Martin, S. J.; Martinand-Mari, C.; Martinet, W.; Martinez-Vicente, M.; Masini, M.; Matarrese, P.; Matsuo, S.; Matteoni, R.; Mayer, A.; Mazure, N. M.; McConkey, D. J.; McConnell, M. J.; McDermott, C.; McDonald, C.; McInerney, G. M.; McKenna, S. L.; McLaughlin, B.; McLean, P. J.; McMaster, C. R.; McQuibban, G. A.; Meijer, A. J.; Meisler, M. H.; Meléndez, A.; Melia, T. J.; Melino, G.; Mena, M. A.; Menendez, J. A.; Menna-Barreto, R. F.; Menon, M. B.; Menzies, F. M.; Mercer, C. A.; Merighi, A.; Merry, D. E.; Meschini, S.; Meyer, C. G.; Meyer, T. F.; Miao, C. Y.; Miao, J. Y.; Michels, P. A.; Michiels, C.; Mijaljica, D.; Milojkovic, A.; Minucci, S.; Miracco, C.; Miranti, C. K.; Mitroulis, I.; Miyazawa, K.; Mizushima, N.; Mograbi, B.; Mohseni, S.; Molero, X.; Mollereau, B.; Mollinedo, F.; Momoi, T.; Monastyrska, I.; Monick, M. M.; Monteiro, M. J.; Moore, M. N.; Mora, R.; Moreau, K.; Moreira, P. I.; Moriyasu, Y.; Moscat, J.; Mostowy, S.; Mottram, J. C.; Motyl, T.; Moussa, C. E.; Müller, S.; Muller, S.; Münger, K.; Münz, C.; Murphy, L. O.; Murphy, M. E.; Mu Sarò, A.; Mysorekar, I.; Nagata, E.; Nagata, K.; Nahimana, A.; Nair, U.; Nakagawa, T.; Nakahira, K.; Nakano, H.; Nakatogawa, H.; Nanjundan, M.; Naqvi, N. I.; Narendra, D. P.; Narita, M.; Navarro, M.; Nawrocki, S. T.; Nazarko, T. Y.; Nemchenko, A.; Netea, M. G.; Neufeld, T. P.; Ney, P. A.; Nezis, I. P.; Nguyen, H. P.; Nie, D.; Nishino, I.; Nislow, C.; Nixon, R. A.; Noda, T.; Noegel, A. A.; Nogalska, A.; Noguchi, S.; Notterpek, L.; Novak, I.; Nozaki, T.; Nukina, N.; Nürnberger, T.; Nyfeler, B.; Obara, K.; Oberley, T. D.; Oddo, S.; Ogawa, M.; Ohashi, T.; Okamoto, K.; Oleinick, N. L.; Oliver, F. J.; Olsen, L. J.; Olsson, S.; Opota, O.; Osborne, T. F.; Ostrander, G. K.; Otsu, K.; Ou, J. H.; Ouimet, M.; Overholtzer, M.; Ozpolat, B.; Paganetti, P.; Pagnini, U.; Pallet, N.; Palmer, G. E.; Palumbo, C.; Pan, T.; Panaretakis, T.; Pandey, U. B.; Papackova, Z.; Papassideri, I.; Paris, I.; Park, J.; Park, O. K.; Parys, J. B.; Parzych, K. R.; Patschan, S.; Patterson, C.; Pattingre, S.; Pawelek, J. M.; Peng, J.; Perlmutter, D. H.; Perrotta, I.; Perry, G.; Pervaiz, S.; Peter, M.; Peters, G. J.; Petersen, M.; Petrovski, G.; Phang, J. M.; Piacentini, M.; Pierre, P.; Pierrefite-Carle, V.; Pierron, G.; Pinkas-Kramarski, R.; Piras, A.; Piri, N.; Platanias, L. C.; Pöggeler, S.; Poirot, M.; Poletti, A.; Poüs, C.; Pozuelo-Rubio, M.; Prætorius-Ibba, M.; Prasad, A.; Prescott, M.; Priault, M.; Produit-Zengaffinen, N.; Progulske-Fox, A.; Proikas-Cezanne, T.; Przedborski, S.; Przyklenk, K.; Puertollano, R.; Puyal, J.; Qian, S. B.; Qin, L.; Qin, Z. H.; Quaggin, S. E.; Raben, N.; Rabinowich, H.; Rabkin, S. W.; Rahman, I.; Rami, A.; Ramm, G.; Randall, G.; Randow, F.; Rao, V. A.; Rathmell, J. C.; Ravikumar, B.; Ray, S. K.; Reed, B. H.; Reed, J. C.; Reggiori, F.; Régnier-Vigouroux, A.; Reichert, A. S.; Reiners, J. J. Jr.; Reiter, R. J.; Ren, J.; Revuelta, J. L.; Rhodes, C. J.; Ritis, K.; Rizzo, E.; Robbins, J.; Roberge, M.; Roca, H.; Roccheri, M. C.; Rocchi, S.; Rodemann, H. P.; Rodríguez De Córdoba, S.; Rohrer, B.; Roninson, I. B.; Rosen, K.; Rost-Roszkowska, M. M.; Rouis, M.; Rouschop, K. M.; Rovetta, F.; Rubin, B. P.; Rubinsztein, D. C.; Ruckdeschel, K.; Rucker, E. B. 3rd.; Rudich, A.; Rudolf, E.; Ruiz-Opazo, N.; Russo, R.; Rusten, T. E.; Ryan, K. M.; Ryter, S. W.; Sabatini, D. M.; Sadoshima, J.; Saha, T.; Saitoh, T.; Sakagami, H.; Sakai, Y.; Salekdeh, G. H.; Salomoni, P.; Salvaterra, P. M.; Salvesen, G.; Salvioli, R.; Sanchez, A. M.; Sánchez-Alcázar, J. A.; Sánchez-Prieto, R.; Sandri, M.; Sankar, U.; Sansanwal, P.; Santambrogio, L.; Saran, S.; Sarkar, S.; Sarwal, M.; Sasakawa, C.; Sasnauskiene, A.; Sass, M.; Sato, K.; Sato, M.; Schapira, A. H.; Scharl, M.; Schätzl, H. M.; Scheper, W.; Schiaffino, S.; Schneider, C.; Schneider, M. E.; Schneider-Stock, R.; Schoenlein, P. V.; Schorderet, D. F.; Schüller, C.; Schwartz, G. K.; Scorrano, L.; Sealy, L.; Seglen, P. O.; Segura-Aguilar, J.; Seiliez, I.; Seleverstov, O.; Sell, C.; Seo, J. B.; Separovic, D.; Setaluri, V.; Setoguchi, T.; Settembre, C.; Shacka, J. J.; Shanmugam, M.; Shapiro, I. M.; Shaulian, E.; Shaw, R. J.; Shelhamer, J. H.; Shen, H. M.; Shen, W. C.; Sheng, Z. H.; Shi, Y.; Shibuya, K.; Shidoji, Y.; Shieh, J. J.; Shih, C. M.; Shimada, Y.; Shimizu, S.; Shintani, T.; Shirihai, O. S.; Shore, G. C.; Sibirny, A. A.; Sidhu, S. B.; Sikorska, B.; Silva-Zacarin, E. C.; Simmons, A.; Simon, A. K.; Simon, H. U.; Simone, C.; Simonsen, A.; Sinclair, D. A.; Singh, R.; Sinha, D.; Sinicrope, F. A.; Sirko, A.; Siu, P. M.; Sivridis, E.; Skop, V.; Skulachev, V. P.; Slack, R. S.; Smaili, S. S.; Smith, D. R.; Soengas, M. S.; Soldati, T.; Song, X.; Sood, A. K.; Soong, T. W.; Sotgia, F.; Spector, S. A.; Spies, C. D.; Springer, W.; Srinivasula, S. M.; Stefanis, L.; Steffan, J. S.; Stendel, R.; Stenmark, H.; Stephanou, A.; Stern, S. T.; Sternberg, C.; Stork, B.; Strålfors, P.; Subauste, C. S.; Sui, X.; Sulzer, D.; Sun, J.; Sun, S. Y.; Sun, Z. J.; Sung, J. J.; Suzuki, K.; Suzuki, T.; Swanson, M. S.; Swanton, C.; Sweeney, S. T.; Sy, L. K.; Szabadkai, G.; Tabas, I.; Taegtmeyer, H.; Tafani, M.; Takács-Vellai, K.; Takano, Y.; Takegawa, K.; Takemura, G.; Takeshita, F.; Talbot, N. J.; Tan, K. S.; Tanaka, K.; Tanaka, K.; Tang, D.; Tang, D.; Tanida, I.; Tannous, B. A.; Tavernarakis, N.; Taylor, G. S.; Taylor, G. A.; Taylor, J. P.; Terada, L. S.; Terman, A.; Tettamanti, G.; Thevissen, K.; Thompson, C. B.; Thorburn, A.; Thumm, M.; Tian, F.; Tian, Y.; Tocchini-Valentini, G.; Tolkovsky, A. M.; Tomino, Y.; Tönges, L.; Tooze, S. A.; Tournier, C.; Tower, J.; Towns, R.; Trajkovic, V.; Travassos, L. H.; Tsai, T. F.; Tschan, M. P.; Tsubata, T.; Tsung, A.; Turk, B.; Turner, L. S.; Tyagi, S. C.; Uchiyama, Y.; Ueno, T.; Umekawa, M.; Umemiya-Shirafuji, R.; Unni, V. K.; Vaccaro, M. I.; Valente, E. M.; Van Den Berghe, G.; Van Der Klei, I. J.; Van Doorn, W.; Van Dyk, L. F.; Van Egmond, M.; Van Grunsven, L. A.; Vandenabeele, P.; Vandenberghe, W. P.; Vanhorebeek, I.; Vaquero, E. C.; Velasco, G.; Vellai, T.; Vicencio, J. M.; Vierstra, R. D.; Vila, M.; Vindis, C.; Viola, G.; Viscomi, M. T.; Voitsekhovskaja, O. V.; Von Haefen, C.; Votruba, M.; Wada, K.; Wade-Martins, R.; Walker, C. L.; Walsh, C. M.; Walter, J.; Wan, X. B.; Wang, A.; Wang, C.; Wang, D.; Wang, F.; Wang, F.; Wang, G.; Wang, H.; Wang, H. G.; Wang, H. D.; Wang, J.; Wang, K.; Wang, M.; Wang, R. C.; Wang, X.; Wang, X.; Wang, Y. J.; Wang, Y.; Wang, Z.; Wang, Z. C.; Wang, Z.; Wansink, D. G.; Ward, D. M.; Watada, H.; Waters, S. L.; Webster, P.; Wei, L.; Weihl, C. C.; Weiss, W. A.; Welford, S. M.; Wen, L. P.; Whitehouse, C. A.; Whitton, J. L.; Whitworth, A. J.; Wileman, T.; Wiley, J. W.; Wilkinson, S.; Willbold, D.; Williams, R. L.; Williamson, P. R.; Wouters, B. G.; Wu, C.; Wu, D. C.; Wu, W. K.; Wyttenbach, A.; Xavier, R. J.; Xi, Z.; Xia, P.; Xiao, G.; Xie, Z.; Xie, Z.; Xu, D. Z.; Xu, J.; Xu, L.; Xu, X.; Yamamoto, A.; Yamamoto, A.; Yamashina, S.; Yamashita, M.; Yan, X.; Yanagida, M.; Yang, D. S.; Yang, E.; Yang, J. M.; Yang, S. Y.; Yang, W.; Yang, W. Y.; Yang, Z.; Yao, M. C.; Yao, T. P.; Yeganeh, B.; Yen, W. L.; Yin, J. J.; Yin, X. M.; Yoo, O. J.; Yoon, G.; Yoon, S. Y.; Yorimitsu, T.; Yoshikawa, Y.; Yoshimori, T.; Yoshimoto, K.; You, H. J.; Youle, R. J.; Younes, A.; Yu, L.; Yu, L.; Yu, S. W.; Yu, W. H.; Yuan, Z. M.; Yue, Z.; Yun, C. H.; Yuzaki, M.; Zabirnyk, O.; Silva-Zacarin, E.; Zacks, D.; Zacksenhaus, E.; Zaffaroni, N.; Zakeri, Z.; Zeh, H. J. 3rd.; Zeitlin, S. O.; Zhang, H.; Zhang, H. L.; Zhang, J.; Zhang, J. P.; Zhang, L.; Zhang, L.; Zhang, M. Y.; Zhang, X. D.; Zhao, M.; Zhao, Y. F.; Zhao, Y.; Zhao, Z. J.; Zheng, X.; Zhivotovsky, B.; Zhong, Q.; Zhou, C. Z.; Zhu, C.; Zhu, W. G.; Zhu, X. F.; Zhu, X.; Zhu, Y.; Zoladek, T.; Zong, W. X.; Zorzano, A.; Zschocke, J.; Zuckerbraun, B. Autophagy. 2012 Apr; 8(4):445-544.
    • (2012) Autophagy , vol.8 , Issue.4 , pp. 445-544
    • Klionsky, D.J.1    Abdalla, F.C.2    Abeliovich, H.3    Abraham, R.T.4    Acevedo-Arozena, A.5    Adeli, K.6    Agholme, L.7    Agnello, M.8    Agostinis, P.9    Aguirre-Ghiso, J.A.10    Ahn, H.J.11    Ait-Mohamed, O.12    Ait-Si-Ali, S.13    Akematsu, T.14    Akira, S.15    Al-Younes, H.M.16    Al-Zeer, M.A.17    Albert, M.L.18    Albin, R.L.19    Alegre-Abarrategui, J.20    more..
  • 47
    • 84862295360 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy
    • Guidelines for the use and interpretation of assays for monitoring autophagy. Autophagy, 2012, 8(4), 445-544.
    • (2012) Autophagy , vol.8 , Issue.4 , pp. 445-544
  • 48
    • 44949159626 scopus 로고    scopus 로고
    • Parkinson's disease and the gut: A well known clinical association in need of an effective cure and explanation
    • Natale, G.; Pasquali, L.; Ruggieri, S.; Paparelli, A.; Fornai, F. Parkinson's disease and the gut: a well known clinical association in need of an effective cure and explanation. Neurogastroenterol. Motil., 2008, 20(7), 741-749.
    • (2008) Neurogastroenterol. Motil. , vol.20 , Issue.7 , pp. 741-749
    • Natale, G.1    Pasquali, L.2    Ruggieri, S.3    Paparelli, A.4    Fornai, F.5
  • 51
    • 48249127948 scopus 로고    scopus 로고
    • Suppression of autophagy precipitates neuronal cell death following low doses of methamphetamine
    • Castino, R.; Lazzeri, G.; Lenzi, P.; Bellio, N.; Follo, C.; Ferrucci, M.; Fornai, F.; Isidoro, C.; Suppression of autophagy precipitates neuronal cell death following low doses of methamphetamine. J. Neurochem., 2008, 106(3), 1426-1439.
    • (2008) J. Neurochem. , vol.106 , Issue.3 , pp. 1426-1439
    • Castino, R.1    Lazzeri, G.2    Lenzi, P.3    Bellio, N.4    Follo, C.5    Ferrucci, M.6    Fornai, F.7    Isidoro, C.8
  • 55
    • 33644859083 scopus 로고    scopus 로고
    • The ubiquitin proteolytic system: From a vague idea, through basic mechanisms, and onto human diseases and drug targeting
    • Ciechanover, A. The ubiquitin proteolytic system: from a vague idea, through basic mechanisms, and onto human diseases and drug targeting. Neurology, 2006, 66(Suppl 1), S7-S19.
    • (2006) Neurology , vol.66 , pp. S7-S19
    • Ciechanover, A.1
  • 56
    • 0033643742 scopus 로고    scopus 로고
    • The ubiquitin-mediated proteolytic pathway: Mode of action and clinical implications
    • Ciechanover, A.; Orian, A.; Schwartz A. L. The ubiquitin-mediated proteolytic pathway: mode of action and clinical implications. J. Cell. Biochem. Suppl., 2000, 34, 40-51.
    • (2000) J. Cell. Biochem. Suppl. , vol.34 , pp. 40-51
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 57
    • 3042723794 scopus 로고    scopus 로고
    • Autophagy: Molecular mechanisms, physiological functions and relevance in human pathology
    • Mariño, G.; López-Otín, C. Autophagy: molecular mechanisms, physiological functions and relevance in human pathology. Cell. Mol. Life Sci., 2004, 61(12), 1439-1454.
    • (2004) Cell. Mol. Life Sci. , vol.61 , Issue.12 , pp. 1439-1454
    • Mariño, G.1    López-Otín, C.2
  • 64
    • 70349612498 scopus 로고    scopus 로고
    • Autophagy for the avoidance of neurodegeneration
    • Madeo, F.; Eisenberg, T.; Kroemer, G. Autophagy for the avoidance of neurodegeneration. Genes Dev., 2009, 23, 2253-2259.
    • (2009) Genes Dev. , vol.23 , pp. 2253-2259
    • Madeo, F.1    Eisenberg, T.2    Kroemer, G.3
  • 66
    • 84869506065 scopus 로고    scopus 로고
    • Role of autophagy inhibitors and inducers in modulating the toxicity of trimethyltin in neuronal cell cultures
    • Fabrizi, C.; Somma, F.; Pompili, E.; Biagioni, F.; Lenzi, P.; Fornai, F.; Fumagalli, L. Role of autophagy inhibitors and inducers in modulating the toxicity of trimethyltin in neuronal cell cultures. J. Neural Transm., 2012, 119(11), 1295-1305.
    • (2012) J. Neural Transm. , vol.119 , Issue.11 , pp. 1295-1305
    • Fabrizi, C.1    Somma, F.2    Pompili, E.3    Biagioni, F.4    Lenzi, P.5    Fornai, F.6    Fumagalli, L.7
  • 67
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine, B.; Kroemer, G. Autophagy in the pathogenesis of disease. Cell., 2008, 132(1), 27-42.
    • (2008) Cell. , vol.132 , Issue.1 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 68
    • 84894350140 scopus 로고    scopus 로고
    • The ER-Golgi intermediate compartment feeds the phagophore membrane
    • Ge, L.; Schekman, R. The ER-Golgi intermediate compartment feeds the phagophore membrane. Autophagy, 2014, 10(1), 170-172.
    • (2014) Autophagy , vol.10 , Issue.1 , pp. 170-172
    • Ge, L.1    Schekman, R.2
  • 71
    • 0036017758 scopus 로고    scopus 로고
    • Induction of autophagy causes dramatic changes in the subcellular distribution of GFPRab24
    • Munafó, D. B.; Colombo, M. I. Induction of autophagy causes dramatic changes in the subcellular distribution of GFPRab24. Traffic, 2002, 3, 472-482.
    • (2002) Traffic , vol.3 , pp. 472-482
    • Munafó, D.B.1    Colombo, M.I.2
  • 72
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells
    • Petiot, A.; Ogier-Denis, E.; Blommaart, E. F.; Meijer, A. J.; Codogno, P. Distinct classes of phosphatidylinositol 3-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells. J. Biol. Chem., 2000, 275, 992-998.
    • (2000) J. Biol. Chem. , vol.275 , pp. 992-998
    • Petiot, A.1    Ogier-Denis, E.2    Blommaart, E.F.3    Meijer, A.J.4    Codogno, P.5
  • 75
    • 33846010776 scopus 로고    scopus 로고
    • Microtubules support production of starvation-induced autophagosomes but not their targeting and fusion with lysosomes
    • Fass, E.; Shvets, E.; Degani, I.; Hirschberg, K.; Elazar, Z. Microtubules support production of starvation-induced autophagosomes but not their targeting and fusion with lysosomes. J. Biol. Chem., 2006, 281(47), 36303-36316.
    • (2006) J. Biol. Chem. , vol.281 , Issue.47 , pp. 36303-36316
    • Fass, E.1    Shvets, E.2    Degani, I.3    Hirschberg, K.4    Elazar, Z.5
  • 76
    • 33645120442 scopus 로고    scopus 로고
    • Microtubules facilitate autophagosome formation and fusion of autophagosomes with endosomes
    • Köchl, R.; Hu, X. W.; Chan, E. Y.; Tooze, S. A. Microtubules facilitate autophagosome formation and fusion of autophagosomes with endosomes. Traffic, 2006, 7(2), 129-145.
    • (2006) Traffic , vol.7 , Issue.2 , pp. 129-145
    • Köchl, R.1    Hu, X.W.2    Chan, E.Y.3    Tooze, S.A.4
  • 77
    • 47149089713 scopus 로고    scopus 로고
    • Dynein-dependent movement of autophagosomes mediates efficient encounters with lysosomes
    • Kimura, S.; Noda, T.; Yoshimori, T. Dynein-dependent movement of autophagosomes mediates efficient encounters with lysosomes. Cell. Struct. Funct., 2008, 33(1), 109-122.
    • (2008) Cell. Struct. Funct. , vol.33 , Issue.1 , pp. 109-122
    • Kimura, S.1    Noda, T.2    Yoshimori, T.3
  • 79
    • 69049112930 scopus 로고    scopus 로고
    • Regulation of endosomal motility and degradation by amyotrophic lateral sclerosis 2/alsin
    • Lai, C.; Xie, C.; Shim, H.; Chandran, J.; Howell, B. W.; Cai, H. Regulation of endosomal motility and degradation by amyotrophic lateral sclerosis 2/alsin. Mol. Brain, 2009, 2, 23.
    • (2009) Mol. Brain , vol.2 , pp. 23
    • Lai, C.1    Xie, C.2    Shim, H.3    Chandran, J.4    Howell, B.W.5    Cai, H.6
  • 80
    • 2642536202 scopus 로고    scopus 로고
    • Alsin is a Rab5 and Rac1 guanine nucleotide exchange factor
    • Topp, J. D.; Gray, N. W.; Gerard, R. D.; Horazdovsky, B. F. Alsin is a Rab5 and Rac1 guanine nucleotide exchange factor. J. Biol. Chem., 2004, 279(23), 24612-24623.
    • (2004) J. Biol. Chem. , vol.279 , Issue.23 , pp. 24612-24623
    • Topp, J.D.1    Gray, N.W.2    Gerard, R.D.3    Horazdovsky, B.F.4
  • 81
    • 4644247430 scopus 로고    scopus 로고
    • Homooligomerization of ALS2 through its unique carboxyl-terminal regions is essential for the ALS2-associated Rab5 guanine nucleotide exchange activity and its regulatory function on endosome trafficking
    • Kunita, R.; Otomo, A.; Mizumura, H.; Suzuki, K.; Showguchi-Miyata, J.; Yanagisawa, Y.; Hadano, S.; Ikeda, J. E. Homooligomerization of ALS2 through its unique carboxyl-terminal regions is essential for the ALS2-associated Rab5 guanine nucleotide exchange activity and its regulatory function on endosome trafficking. J. Biol. Chem., 2004, 279(37), 38626-38635.
    • (2004) J. Biol. Chem. , vol.279 , Issue.37 , pp. 38626-38635
    • Kunita, R.1    Otomo, A.2    Mizumura, H.3    Suzuki, K.4    Showguchi-Miyata, J.5    Yanagisawa, Y.6    Hadano, S.7    Ikeda, J.E.8
  • 82
    • 0036696804 scopus 로고    scopus 로고
    • Escrt-III: An endosome-associated heterooligomeric protein complex required for mvb sorting
    • Babst, M.; Katzmann, D. J.; Estepa-Sabal, E. J.; Meerloo, T.; Emr, S. D. Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting. Dev. Cell., 2002, 3, 271-282.
    • (2002) Dev. Cell. , vol.3 , pp. 271-282
    • Babst, M.1    Katzmann, D.J.2    Estepa-Sabal, E.J.3    Meerloo, T.4    Emr, S.D.5
  • 83
    • 0036697166 scopus 로고    scopus 로고
    • Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body
    • Babst, M.; Katzmann, D. J.; Snyder, W. B.; Wendland, B.; Emr, S. D. Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body. Dev. Cell., 2002, 3, 283-289.
    • (2002) Dev. Cell. , vol.3 , pp. 283-289
    • Babst, M.1    Katzmann, D.J.2    Snyder, W.B.3    Wendland, B.4    Emr, S.D.5
  • 84
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • Babst, M.; Wendland, B.; Estepa, E, J.; Emr, S. D. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J., 1998, 17(11), 2982-2993.
    • (1998) EMBO J. , vol.17 , Issue.11 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 85
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • Katzmann, D. J.; Babst, M.; Emr, S. D. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell., 2001, 106, 145-155.
    • (2001) Cell. , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 86
    • 33646010475 scopus 로고    scopus 로고
    • The ESCRT complexes: Structure and mechanism of a membrane-trafficking network
    • Hurley, J. H.; Emr, S. D. The ESCRT complexes: structure and mechanism of a membrane-trafficking network. Annu. Rev. Biophys. Biomol. Struct., 2006, 35, 277-298.
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 277-298
    • Hurley, J.H.1    Emr, S.D.2
  • 87
    • 33744985540 scopus 로고    scopus 로고
    • Endosomal and non-endosomal functions of ESCRT proteins
    • Slagsvold, T.; Pattni, K.; Malerød, L.; Stenmark, H. Endosomal and non-endosomal functions of ESCRT proteins. Trends Cell. Biol., 2006, 16(6), 317-326.
    • (2006) Trends Cell. Biol. , vol.16 , Issue.6 , pp. 317-326
    • Slagsvold, T.1    Pattni, K.2    Malerød, L.3    Stenmark, H.4
  • 88
    • 34247342216 scopus 로고    scopus 로고
    • The emerging shape of the ESCRT machinery
    • Williams, R, L.; Urbé, S. The emerging shape of the ESCRT machinery. Nat. Rev. Mol. Cell. Biol., 2007, 8(5), 355-368.
    • (2007) Nat. Rev. Mol. Cell. Biol. , vol.8 , Issue.5 , pp. 355-368
    • Williams, R.L.1    Urbé, S.2
  • 90
    • 39049148153 scopus 로고    scopus 로고
    • Aggresome formation and neurodegenerative diseases: Therapeutic implications
    • Olzmann, J. A.; Li, L.; Chin, L. S. Aggresome formation and neurodegenerative diseases: therapeutic implications. Curr. Med. Chem. 2008, 15(1), 47-60.
    • (2008) Curr. Med. Chem , vol.15 , Issue.1 , pp. 47-60
    • Olzmann, J.A.1    Li, L.2    Chin, L.S.3
  • 91
    • 0005677775 scopus 로고
    • 3-Methyladenine. Specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes
    • Seglen, P. O.; Gordon, P. B. 3-Methyladenine. Specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes. Proc. Natl. Acad. Sci. USA, 1982, 79(6), 1889-1892.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , Issue.6 , pp. 1889-1892
    • Seglen, P.O.1    Gordon, P.B.2
  • 92
    • 0347986620 scopus 로고    scopus 로고
    • Class III phosphoinositide 3-kinase-beclin1 complex mediates the amino aciddependent regulation of autophagy in C2C12 myotubes
    • Tassa, A.; Roux, M. P.; Attaix, D.; Bechet, D. M. Class III phosphoinositide 3-kinase-beclin1 complex mediates the amino aciddependent regulation of autophagy in C2C12 myotubes. Biochem. J., 2003, 376, 577-586.
    • (2003) Biochem. J. , vol.376 , pp. 577-586
    • Tassa, A.1    Roux, M.P.2    Attaix, D.3    Bechet, D.M.4
  • 94
  • 95
    • 33749052075 scopus 로고    scopus 로고
    • Signalling and autophagy regulation in health, aging and disease
    • Meijer, A. J.; Codogno, P. Signalling and autophagy regulation in health, aging and disease. Mol. Aspects Med., 2006, 27(5-6), 411-425.
    • (2006) Mol. Aspects Med. , vol.27 , Issue.5-6 , pp. 411-425
    • Meijer, A.J.1    Codogno, P.2
  • 97
    • 34250894388 scopus 로고    scopus 로고
    • BH3-only proteins and BH3 mimetics induce autophagy by competitively disrupting the interaction between Beclin 1 and Bcl-2/Bcl-X (L)
    • Maiuri, M. C.; Criollo, A.; Tasdemir, E.; Vicencio, J. M.; Tajeddine, N.; Hickman, J. A.; Geneste, O.; Kroemer G. BH3-only proteins and BH3 mimetics induce autophagy by competitively disrupting the interaction between Beclin 1 and Bcl-2/Bcl-X (L). Autophagy., 2007, 3(4), 374-376.
    • (2007) Autophagy. , vol.3 , Issue.4 , pp. 374-376
    • Maiuri, M.C.1    Criollo, A.2    Tasdemir, E.3    Vicencio, J.M.4    Tajeddine, N.5    Hickman, J.A.6    Geneste, O.7    Kroemer, G.8
  • 101
    • 84894313670 scopus 로고    scopus 로고
    • Autophagy reduces neuronal damage and promotes locomotor recovery via inhibition of apoptosis after spinal cord injury in rats
    • in press
    • Tang, P.; Hou, H.; Zhang, L.; Lan, X.; Mao, Z.; Liu, D.; He, C.; Du, H.; Zhang, L. Autophagy Reduces Neuronal Damage and Promotes Locomotor Recovery via Inhibition of Apoptosis After Spinal Cord Injury in Rats. Mol. Neurobiol., 2013, in press. doi: 10.1007/s12035-013-8615-3.
    • (2013) Mol. Neurobiol.
    • Tang, P.1    Hou, H.2    Zhang, L.3    Lan, X.4    Mao, Z.5    Liu, D.6    He, C.7    Du, H.8    Zhang, L.9
  • 104
    • 0035809160 scopus 로고    scopus 로고
    • Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae
    • Kihara, A.; Noda, T.; Ishihara, N.; Ohsumi, Y. Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae. J. Cell. Biol., 2001, 152(3), 519-530.
    • (2001) J. Cell. Biol. , vol.152 , Issue.3 , pp. 519-530
    • Kihara, A.1    Noda, T.2    Ishihara, N.3    Ohsumi, Y.4
  • 105
    • 0026100188 scopus 로고
    • Familial amyotrophic lateral sclerosis, 1850-1989: A statistical analysis of the world literature
    • Strong, M. J.; Hudson, A. J.; Alvord, W. G. Familial amyotrophic lateral sclerosis, 1850-1989: a statistical analysis of the world literature. Can. J. Neurol. Sci., 1991, 18(1), 45-58.
    • (1991) Can. J. Neurol. Sci. , vol.18 , Issue.1 , pp. 45-58
    • Strong, M.J.1    Hudson, A.J.2    Alvord, W.G.3
  • 106
    • 0042632880 scopus 로고    scopus 로고
    • Genetic epidemiology of amyotrophic lateral sclerosis
    • Majoor-Krakauer, D.; Willems, P. J.; Hofman, A. Genetic epidemiology of amyotrophic lateral sclerosis. Clin. Genet., 2003, 63(2), 83-101.
    • (2003) Clin. Genet. , vol.63 , Issue.2 , pp. 83-101
    • Majoor-Krakauer, D.1    Willems, P.J.2    Hofman, A.3
  • 109
    • 41449113885 scopus 로고    scopus 로고
    • Altered macroautophagy in the spinal cord of SOD1 mutant mice
    • Li, L.; Zhang, X.; Le, W. Altered macroautophagy in the spinal cord of SOD1 mutant mice. Autophagy, 2008, 4, 290-293.
    • (2008) Autophagy , vol.4 , pp. 290-293
    • Li, L.1    Zhang, X.2    Le, W.3
  • 110
    • 80052353946 scopus 로고    scopus 로고
    • In vivo optical imaging of motor neuron autophagy in a mouse model of amyotrophic lateral sclerosis
    • Tian, F.; Morimoto, N.; Liu, W.; Ohta, Y.; Deguchi, K.; Miyazaki, K.; Abe, K. In vivo optical imaging of motor neuron autophagy in a mouse model of amyotrophic lateral sclerosis. Autophagy, 2011, 7, 985-992.
    • (2011) Autophagy , vol.7 , pp. 985-992
    • Tian, F.1    Morimoto, N.2    Liu, W.3    Ohta, Y.4    Deguchi, K.5    Miyazaki, K.6    Abe, K.7
  • 111
    • 84902550621 scopus 로고    scopus 로고
    • Oxidative stress and autophagic alteration in brainstem of SOD1-G93A mouse model of ALS
    • in press
    • An, T.; Shi, P.; Duan, W.; Zhang, S.; Yuan, P.; Li, Z.; Wu, D.; Xu, Z.; Li, C.; Guo, Y. Oxidative Stress and Autophagic Alteration in Brainstem of SOD1-G93A Mouse Model of ALS. Mol Neurobiol., 2014, in press. doi 10.1007/s12035-013-8623-3.
    • (2014) Mol Neurobiol.
    • An, T.1    Shi, P.2    Duan, W.3    Zhang, S.4    Yuan, P.5    Li, Z.6    Wu, D.7    Xu, Z.8    Li, C.9    Guo, Y.10
  • 112
    • 33750089740 scopus 로고    scopus 로고
    • Degradation of amyotrophic lateral sclerosis-linked mutant Cu, Zn superoxide dismutase proteins by macroautophagy and the proteasome
    • Kabuta, T.; Suzuki, Y.; Wada, K. Degradation of amyotrophic lateral sclerosis-linked mutant Cu, Zn superoxide dismutase proteins by macroautophagy and the proteasome. J. Biol. Chem., 2006, 281, 30524-30533.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30524-30533
    • Kabuta, T.1    Suzuki, Y.2    Wada, K.3
  • 115
    • 70350131893 scopus 로고    scopus 로고
    • Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin-independent mechanism
    • Gal, J.; Ström, A. L.; Kwinter, D. M.; Kilty, R.; Zhang, J.; Shi, P.; Fu, W.; Wooten, M. W.; Zhu, H. Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin-independent mechanism. J. Neurochem., 2009, 111(4), 1062-1073.
    • (2009) J. Neurochem. , vol.111 , Issue.4 , pp. 1062-1073
    • Gal, J.1    Ström, A.L.2    Kwinter, D.M.3    Kilty, R.4    Zhang, J.5    Shi, P.6    Fu, W.7    Wooten, M.W.8    Zhu, H.9
  • 117
    • 34249679116 scopus 로고    scopus 로고
    • p62 accumulates and enhances aggregate formation in model systems of familial amyotrophic lateral sclerosis
    • Gal, J.; Strom, A. L.; Kilty, R.; Zhang, F.; Zhu, H. p62 accumulates and enhances aggregate formation in model systems of familial amyotrophic lateral sclerosis. J. Biol. Chem., 2007, 282(15), 11068-11077.
    • (2007) J. Biol. Chem. , vol.282 , Issue.15 , pp. 11068-11077
    • Gal, J.1    Strom, A.L.2    Kilty, R.3    Zhang, F.4    Zhu, H.5
  • 118
    • 34447550238 scopus 로고    scopus 로고
    • Interaction between familial amyotrophic lateral sclerosis (ALS) - Linked SOD1 mutants and the dynein complex
    • Hang, F.; Strom, A. L.; Fukada, K.; Lee, S.; Hayward, L. J.; Zhu, H. Interaction between familial amyotrophic lateral sclerosis (ALS) - linked SOD1 mutants and the dynein complex. J. Biol. Chem., 2007, 282, 16691-16699.
    • (2007) J. Biol. Chem. , vol.282 , pp. 16691-16699
    • Hang, F.1    Strom, A.L.2    Fukada, K.3    Lee, S.4    Hayward, L.J.5    Zhu, H.6
  • 122
    • 0025974686 scopus 로고
    • Rab5 controls early endosome fusion in vitro
    • Gorvel, J. P.; Chavrier, P.; Zerial, M.; Gruenberg, J. Rab5 controls early endosome fusion in vitro. Cell, 1991, 64(5), 915-925.
    • (1991) Cell , vol.64 , Issue.5 , pp. 915-925
    • Gorvel, J.P.1    Chavrier, P.2    Zerial, M.3    Gruenberg, J.4
  • 123
    • 0031983836 scopus 로고    scopus 로고
    • A novel role for Rab5-GDI in ligand sequestration into clathrin-coated pits
    • McLauchlan, H.; Newell, J.; Morrice, N.; Osborne, A.; West, M.; Smythe, E. A novel role for Rab5-GDI in ligand sequestration into clathrin-coated pits. Curr. Biol., 1998, 8(1), 34-45.
    • (1998) Curr. Biol. , vol.8 , Issue.1 , pp. 34-45
    • McLauchlan, H.1    Newell, J.2    Morrice, N.3    Osborne, A.4    West, M.5    Smythe, E.6
  • 125
    • 20444410032 scopus 로고    scopus 로고
    • Caenorhabditis elegans RME-6 is a novel regulator of RAB-5 at the clathrin-coated pit
    • Sato, M.; Sato, K.; Fonarev, P.; Huang, C. J.; Liou, W.; Grant, B. D. Caenorhabditis elegans RME-6 is a novel regulator of RAB-5 at the clathrin-coated pit. Nat. Cell. Biol., 2005, 7(6), 559-569.
    • (2005) Nat. Cell. Biol. , vol.7 , Issue.6 , pp. 559-569
    • Sato, M.1    Sato, K.2    Fonarev, P.3    Huang, C.J.4    Liou, W.5    Grant, B.D.6
  • 126
    • 34447531775 scopus 로고    scopus 로고
    • The Rab5 activator ALS2/alsin acts as a novel Rac1 effector through Rac1-activated endocytosis
    • Kunita, R.; Otomo, A.; Mizumura, H.; Suzuki-Utsunomiya, K.; Hadano, S.; Ikeda, J. E. The Rab5 activator ALS2/alsin acts as a novel Rac1 effector through Rac1-activated endocytosis. J. Biol. Chem., 2007, 282, 16599-16611.
    • (2007) J. Biol. Chem. , vol.282 , pp. 16599-16611
    • Kunita, R.1    Otomo, A.2    Mizumura, H.3    Suzuki-Utsunomiya, K.4    Hadano, S.5    Ikeda, J.E.6
  • 127
    • 79952317005 scopus 로고    scopus 로고
    • Defective relocalization of ALS2/alsin missense mutants to Rac1-induced macropinosomes accounts for loss of their cellular function and leads to disturbed amphisome formation
    • Otomo, A.; Kunita, R.; Suzuki-Utsunomiya, K.; Ikeda, J. E.; Hadano. S. Defective relocalization of ALS2/alsin missense mutants to Rac1-induced macropinosomes accounts for loss of their cellular function and leads to disturbed amphisome formation. FEBS Lett., 2011, 585(5), 730-736.
    • (2011) FEBS Lett. , vol.585 , Issue.5 , pp. 730-736
    • Otomo, A.1    Kunita, R.2    Suzuki-Utsunomiya, K.3    Ikeda, J.E.4    Hadano, S.5
  • 133
    • 0026345013 scopus 로고
    • Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein
    • Gill, S. R.; Schroer, T. A.; Szilak, I.; Steuer, E. R.; Sheetz, M. P.; Cleveland, D. W. Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein. J. Cell. Biol., 1991, 115(6), 1639-1650.
    • (1991) J. Cell. Biol. , vol.115 , Issue.6 , pp. 1639-1650
    • Gill, S.R.1    Schroer, T.A.2    Szilak, I.3    Steuer, E.R.4    Sheetz, M.P.5    Cleveland, D.W.6
  • 134
    • 0025789647 scopus 로고
    • Two activators of microtubule-based vesicle transport
    • Schroer, T. A.; Sheetz, M. P. Two activators of microtubule-based vesicle transport. J. Cell. Biol., 1991, 115(5), 1309-1318.
    • (1991) J. Cell. Biol. , vol.115 , Issue.5 , pp. 1309-1318
    • Schroer, T.A.1    Sheetz, M.P.2
  • 137
    • 79955949858 scopus 로고    scopus 로고
    • The elimination of accumulated and aggregated proteins: A role for aggrephagy in neurodegeneration
    • Yamamoto, A.; Simonsen, A. The elimination of accumulated and aggregated proteins: a role for aggrephagy in neurodegeneration. Neurobiol. Dis., 2011, 43, 17-28.
    • (2011) Neurobiol. Dis. , vol.43 , pp. 17-28
    • Yamamoto, A.1    Simonsen, A.2
  • 139
    • 50849110466 scopus 로고    scopus 로고
    • A novel mouse model with impaired dynein/dynactin function develops amyotrophic lateral sclerosis (ALS)-like features in motor neurons and improves lifespan in SOD1-ALS mice
    • Teuling, E.; Van Dis, V.; Wulf, P. S.; Haasdijk, E. D.; Akhmanova, A.; Hoogenraad, C. C.; Jaarsma, D. A novel mouse model with impaired dynein/dynactin function develops amyotrophic lateral sclerosis (ALS)-like features in motor neurons and improves lifespan in SOD1-ALS mice. Hum. Mol. Genet., 2008, 17(18), 2849-2862.
    • (2008) Hum. Mol. Genet. , vol.17 , Issue.18 , pp. 2849-2862
    • Teuling, E.1    Van Dis, V.2    Wulf, P.S.3    Haasdijk, E.D.4    Akhmanova, A.5    Hoogenraad, C.C.6    Jaarsma, D.7
  • 140
    • 74949114469 scopus 로고    scopus 로고
    • The effects of dynein inhibition on the autophagic pathway in glioma cells
    • Yamamoto, M.; Suzuki, S. O.; Himeno, M. The effects of dynein inhibition on the autophagic pathway in glioma cells. Neuropathology, 2010, 30(1), 1-6.
    • (2010) Neuropathology , vol.30 , Issue.1 , pp. 1-6
    • Yamamoto, M.1    Suzuki, S.O.2    Himeno, M.3
  • 143
    • 34548492271 scopus 로고    scopus 로고
    • ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration
    • Lee, J. A.; Beigneux, A.; Ahmad, S. T.; Young, S. G.; Gao, F. B. ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration. Curr. Biol., 2007, 17(18), 1561-1567.
    • (2007) Curr. Biol. , vol.17 , Issue.18 , pp. 1561-1567
    • Lee, J.A.1    Beigneux, A.2    Ahmad, S.T.3    Young, S.G.4    Gao, F.B.5
  • 145
    • 67649996222 scopus 로고    scopus 로고
    • Inhibition of autophagy induction delays neuronal cell loss caused by dysfunctional ESCRT-III in frontotemporal dementia
    • Lee, J. A.; Gao, F. B. Inhibition of autophagy induction delays neuronal cell loss caused by dysfunctional ESCRT-III in frontotemporal dementia. J. Neurosci., 2009, 29, 8506-8511.
    • (2009) J. Neurosci. , vol.29 , pp. 8506-8511
    • Lee, J.A.1    Gao, F.B.2
  • 146
    • 84890613856 scopus 로고    scopus 로고
    • Interactions between endosomal maturation and autophagy: Analysis of ESCRT machinery during caenorhabditis elegans development
    • Manil-Ségalen, M.; Culetto, E.; Legouis, R.; Lefebvre, C. Interactions Between Endosomal Maturation and Autophagy: Analysis of ESCRT Machinery During Caenorhabditis elegans Development. Methods Enzymol., 2014, 534, 93-118.
    • (2014) Methods Enzymol. , vol.534 , pp. 93-118
    • Manil-Ségalen, M.1    Culetto, E.2    Legouis, R.3    Lefebvre, C.4
  • 147
    • 84858119593 scopus 로고    scopus 로고
    • Induction of autophagy in ESCRT mutants is an adaptive response for cell survival in C. Elegans
    • Djeddi, A.; Michelet, X.; Culetto, E.; Alberti, A.; Barois, N.; Legouis, R. Induction of autophagy in ESCRT mutants is an adaptive response for cell survival in C. elegans. J. Cell. Sci. 2012, 125(Pt 3), 685-694.
    • (2012) J. Cell. Sci , vol.125 , pp. 685-694
    • Djeddi, A.1    Michelet, X.2    Culetto, E.3    Alberti, A.4    Barois, N.5    Legouis, R.6
  • 148
    • 69449089915 scopus 로고    scopus 로고
    • How do ESCRT proteins control autophagy?
    • Rusten, T. E.; Stenmark, H. How do ESCRT proteins control autophagy? J. Cell. Sci., 2009, 122(Pt 13), 2179-2183.
    • (2009) J. Cell. Sci. , vol.122 , pp. 2179-2183
    • Rusten, T.E.1    Stenmark, H.2
  • 149
    • 84886294903 scopus 로고    scopus 로고
    • Syntaxin 13, a genetic modifier of mutant CHMP2B in frontotemporal dementia, is required for autophagosome maturation
    • Lu, Y.; Zhang, Z.; Sun, D.; Sweeney, S. T.; Gao, F. B. Syntaxin 13, a genetic modifier of mutant CHMP2B in frontotemporal dementia, is required for autophagosome maturation. Mol. Cell., 2013, 52(2), 264-271.
    • (2013) Mol. Cell. , vol.52 , Issue.2 , pp. 264-271
    • Lu, Y.1    Zhang, Z.2    Sun, D.3    Sweeney, S.T.4    Gao, F.B.5
  • 150
    • 79960774898 scopus 로고    scopus 로고
    • Autophagosome precursor maturation requires homotypic fusion
    • Moreau, K.; Ravikumar, B.; Renna, M.; Puri, C.; Rubinsztein, D. C. Autophagosome precursor maturation requires homotypic fusion. Cell., 2011, 146(2), 303-317.
    • (2011) Cell. , vol.146 , Issue.2 , pp. 303-317
    • Moreau, K.1    Ravikumar, B.2    Renna, M.3    Puri, C.4    Rubinsztein, D.C.5
  • 153
    • 77649252528 scopus 로고    scopus 로고
    • Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis
    • Pesiridis, G. S.; Lee, V. M.; Trojanowski, J. Q. Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis. Hum. Mol. Genet., 2009, 18(R2), R156-162.
    • (2009) Hum. Mol. Genet. , vol.18 , Issue.R2 , pp. R156-R162
    • Pesiridis, G.S.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 158
    • 77954372835 scopus 로고    scopus 로고
    • Protein aggregation and defective RNA metabolism as mechanisms for motor neuron damage
    • Ticozzi, N.; Ratti, A.; Silani, V. Protein aggregation and defective RNA metabolism as mechanisms for motor neuron damage. CNS Neurol. Disord. Drug Targets, 2010, 9(3), 285-296.
    • (2010) CNS Neurol. Disord. Drug Targets , vol.9 , Issue.3 , pp. 285-296
    • Ticozzi, N.1    Ratti, A.2    Silani, V.3
  • 159
    • 77949897022 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis and frontotemporal lobar degeneration: A spectrum of TDP-43 proteinopathies
    • Geser, F.; Lee, V. M.; Trojanowski, J. Q. Amyotrophic lateral sclerosis and frontotemporal lobar degeneration: a spectrum of TDP-43 proteinopathies. Neuropathology, 2010, 30(2), 103-112
    • (2010) Neuropathology , vol.30 , Issue.2 , pp. 103-112
    • Geser, F.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 161
    • 72649087184 scopus 로고    scopus 로고
    • Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system
    • Wang, X.; Fan, H.; Ying, Z.; Li, B.; Wang, H.; Wang, G. Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system. Neurosci. Lett., 2010, 469(1), 112-116.
    • (2010) Neurosci. Lett. , vol.469 , Issue.1 , pp. 112-116
    • Wang, X.1    Fan, H.2    Ying, Z.3    Li, B.4    Wang, H.5    Wang, G.6
  • 162
    • 84866289381 scopus 로고    scopus 로고
    • Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43
    • Wang, I. F.; Guo, B. S.; Liu, Y. C.; Wu, C. C.; Yang, C. H.; Tsai, K. J.; Shen, C. K. Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43. Proc. Natl. Acad. Sci. U. S. A., 2012, 109(37), 15024-15029.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , Issue.37 , pp. 15024-15029
    • Wang, I.F.1    Guo, B.S.2    Liu, Y.C.3    Wu, C.C.4    Yang, C.H.5    Tsai, K.J.6    Shen, C.K.7
  • 163
    • 84873628557 scopus 로고    scopus 로고
    • Autophagy activation ameliorates neuronal pathogenesis of FTLD-U mice: A new light for treatment of TARDBP/TDP-43 proteinopathies
    • Wang, I. F.; Tsai, K. J.; Shen, C. K. Autophagy activation ameliorates neuronal pathogenesis of FTLD-U mice: a new light for treatment of TARDBP/TDP-43 proteinopathies. Autophagy, 2013, 9(2), 239-240.
    • (2013) Autophagy , vol.9 , Issue.2 , pp. 239-240
    • Wang, I.F.1    Tsai, K.J.2    Shen, C.K.3
  • 165
    • 84455169931 scopus 로고    scopus 로고
    • Regulation of autophagy by neuropathological protein TDP-43
    • Bose, J. K.; Huang, C. C.; Shen, C. K. Regulation of autophagy by neuropathological protein TDP-43. J. Biol. Chem., 2011, 286(52), 44441-44448.
    • (2011) J. Biol. Chem. , vol.286 , Issue.52 , pp. 44441-44448
    • Bose, J.K.1    Huang, C.C.2    Shen, C.K.3
  • 169
  • 171
    • 38949162988 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitin potentially partners with p62 to promote the clearance of protein inclusions by autophagy
    • Tan, J. M.; Wong, E. S.; Dawson, V. L.; Dawson, T. M.; Lim, K. L. Lysine 63-linked polyubiquitin potentially partners with p62 to promote the clearance of protein inclusions by autophagy. Autophagy, 2008, 4(2), 251-253.
    • (2008) Autophagy , vol.4 , Issue.2 , pp. 251-253
    • Tan, J.M.1    Wong, E.S.2    Dawson, V.L.3    Dawson, T.M.4    Lim, K.L.5
  • 172
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjørkøy, G.; Lamark, T.; Brech, A.; Outzen, H.; Perander, M.; Overvatn, A.; Stenmark, H.; Johansen, T. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell. Biol., 2005, 171(4), 603-614.
    • (2005) J. Cell. Biol. , vol.171 , Issue.4 , pp. 603-614
    • Bjørkøy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 173
    • 33645926989 scopus 로고    scopus 로고
    • p62/SQSTM1: A missing link between protein aggregates and the autophagy machinery
    • Bjørkøy, G.; Lamark, T.; Johansen, T. p62/SQSTM1: a missing link between protein aggregates and the autophagy machinery. Autophagy, 2006, 2(2), 138-139.
    • (2006) Autophagy , vol.2 , Issue.2 , pp. 138-139
    • Bjørkøy, G.1    Lamark, T.2    Johansen, T.3
  • 174
    • 0034649661 scopus 로고    scopus 로고
    • FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis
    • Hattula, K.; Peranen, J. FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis. Curr. Biol., 2000, 10, 1603-1606.
    • (2000) Curr. Biol. , vol.10 , pp. 1603-1606
    • Hattula, K.1    Peranen, J.2
  • 175
    • 27144523294 scopus 로고    scopus 로고
    • Inhibition of metabotropic glutamate receptor signaling by the huntingtin-binding protein optineurin
    • Anborgh, P. H.; Godin, C.; Pampillo, M.; Dhami, G. K.; Dale, L. B.; Cregan, S. P.; Truant, R.; Ferguson, S. S. Inhibition of metabotropic glutamate receptor signaling by the huntingtin-binding protein optineurin. J. Biol. Chem., 2005, 280(41), 34840-34848.
    • (2005) J. Biol. Chem. , vol.280 , Issue.41 , pp. 34840-34848
    • Anborgh, P.H.1    Godin, C.2    Pampillo, M.3    Dhami, G.K.4    Dale, L.B.5    Cregan, S.P.6    Truant, R.7    Ferguson, S.S.8
  • 177
    • 34547924464 scopus 로고    scopus 로고
    • Optineurin negatively regulates TNFalpha-induced NF-kappaB activation by competing with NEMO for ubiquitinated RIP
    • Zhu, G.; Wu, C. J.; Zhao, Y.; Ashwell, J. D. Optineurin negatively regulates TNFalpha-induced NF-kappaB activation by competing with NEMO for ubiquitinated RIP. Curr. Biol., 2007, 17(16), 1438-1443.
    • (2007) Curr. Biol. , vol.17 , Issue.16 , pp. 1438-1443
    • Zhu, G.1    Wu, C.J.2    Zhao, Y.3    Ashwell, J.D.4
  • 178
    • 65249141171 scopus 로고    scopus 로고
    • Mutant huntingtin impairs post-Golgi trafficking to lysosomes by delocalizing optineurin/Rab8 complex from the Golgi apparatus
    • Del Toro, D.; Alberch, J.; Lázaro-Diéguez, F.; Martín-Ibáñez, R.; Xifró, X.; Egea, G.; Canals, J. M. Mutant huntingtin impairs post-Golgi trafficking to lysosomes by delocalizing optineurin/Rab8 complex from the Golgi apparatus. Mol. Biol. Cell., 2009, 20(5), 1478-1492.
    • (2009) Mol. Biol. Cell. , vol.20 , Issue.5 , pp. 1478-1492
    • Del Toro, D.1    Alberch, J.2    Lázaro-Diéguez, F.3    Martín-Ibáñez, R.4    Xifró, X.5    Egea, G.6    Canals, J.M.7
  • 179
    • 84857437068 scopus 로고    scopus 로고
    • Plk1-dependent phosphorylation of optineurin provides a negative feedback mechanism for mitotic progression
    • Kachaner, D.; Filipe, J.; Laplantine, E.; Bauch, A.; Bennett, K. L.; Superti-Furga, G.; Israël, A.; Weil, R. Plk1-dependent phosphorylation of optineurin provides a negative feedback mechanism for mitotic progression. Mol. Cell., 2012, 45(4), 553-566.
    • (2012) Mol. Cell. , vol.45 , Issue.4 , pp. 553-566
    • Kachaner, D.1    Filipe, J.2    Laplantine, E.3    Bauch, A.4    Bennett, K.L.5    Superti-Furga, G.6    Israël, A.7    Weil, R.8
  • 180
  • 181
    • 68349104931 scopus 로고    scopus 로고
    • Optineurin and its mutants: Molecules associated with some forms of glaucoma
    • Chalasani, M. L.; Swarup, G.; Balasubramanian, D. Optineurin and its mutants: molecules associated with some forms of glaucoma. Ophthalmic Res., 2009, 42(4), 176-184.
    • (2009) Ophthalmic Res. , vol.42 , Issue.4 , pp. 176-184
    • Chalasani, M.L.1    Swarup, G.2    Balasubramanian, D.3
  • 190
    • 2442520399 scopus 로고    scopus 로고
    • Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitinassociated and ubiquitin-like domains
    • Ko, H. S.; Uehara, T.; Tsuruma, K.; Nomura, Y. Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitinassociated and ubiquitin-like domains. FEBS Lett., 2004, 566, 110-114.
    • (2004) FEBS Lett. , vol.566 , pp. 110-114
    • Ko, H.S.1    Uehara, T.2    Tsuruma, K.3    Nomura, Y.4
  • 194
    • 20144389039 scopus 로고    scopus 로고
    • Occurrence of neuronal inclusions combined with increased nigral expression of alpha-synuclein within dopaminergic neurons following treatment with amphetamine derivatives in mice
    • Fornai, F.; Lenzi, P.; Ferrucci, M.; Lazzeri, G.; Bandettini Di Poggio, A.; Natale, G.; Busceti, C. L.; Biagioni, F.; Giusiani, M.; Ruggieri, S.; Paparelli, A. Occurrence of neuronal inclusions combined with increased nigral expression of alpha-synuclein within dopaminergic neurons following treatment with amphetamine derivatives in mice. Brain Res. Bull., 2005, 65(5), 405-413.
    • (2005) Brain Res. Bull. , vol.65 , Issue.5 , pp. 405-413
    • Fornai, F.1    Lenzi, P.2    Ferrucci, M.3    Lazzeri, G.4    Bandettini Di Poggio, A.5    Natale, G.6    Busceti, C.L.7    Biagioni, F.8    Giusiani, M.9    Ruggieri, S.10    Paparelli, A.11
  • 195
    • 33747141059 scopus 로고    scopus 로고
    • The neurotoxicity of amphetamines: Bridging drugs of abuse and neurodegenerative disorders
    • Iacovelli, L.; Fulceri, F.; De Blasi, A.; Nicoletti, F.; Ruggieri, S.; Fornai, F. The neurotoxicity of amphetamines: bridging drugs of abuse and neurodegenerative disorders. Exp. Neurol., 2006, 201(1), 24-31.
    • (2006) Exp. Neurol. , vol.201 , Issue.1 , pp. 24-31
    • Iacovelli, L.1    Fulceri, F.2    De Blasi, A.3    Nicoletti, F.4    Ruggieri, S.5    Fornai, F.6
  • 196
    • 53549108890 scopus 로고    scopus 로고
    • Analysis of single, purified inclusions as a novel approach to understand methamphetamine neurotoxicity
    • Lenzi, P.; Fulceri, F.; Lazzeri, G.; Casini, A.; Ruggieri, S.; Paparelli, A.; Fornai, F. Analysis of single, purified inclusions as a novel approach to understand methamphetamine neurotoxicity. Ann. N. Y. Acad. Sci., 2008, 1139, 186-190.
    • (2008) Ann. N. Y. Acad. Sci. , vol.1139 , pp. 186-190
    • Lenzi, P.1    Fulceri, F.2    Lazzeri, G.3    Casini, A.4    Ruggieri, S.5    Paparelli, A.6    Fornai, F.7
  • 197
    • 80054024011 scopus 로고    scopus 로고
    • Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
    • Jucker, M.; Walker, L. C. Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders. Ann. Neurol., 2011, 70, 532-540.
    • (2011) Ann. Neurol. , vol.70 , pp. 532-540
    • Jucker, M.1    Walker, L.C.2
  • 198
    • 0034726119 scopus 로고    scopus 로고
    • Alphasynuclein immunoreactivity of huntingtin polyglutamine aggregates in striatum and cortex of Huntington's disease patients and transgenic mouse models
    • Charles, V.; Mezey, E.; Reddy, P. H.; Dehejia, A.; Young, T. A.; Polymeropoulos, M. H.; Brownstein, M.; Tagle, D. A. Alphasynuclein immunoreactivity of huntingtin polyglutamine aggregates in striatum and cortex of Huntington's disease patients and transgenic mouse models. Neurosci. Lett., 2000, 289(1), 29-32.
    • (2000) Neurosci. Lett. , vol.289 , Issue.1 , pp. 29-32
    • Charles, V.1    Mezey, E.2    Reddy, P.H.3    Dehejia, A.4    Young, T.A.5    Polymeropoulos, M.H.6    Brownstein, M.7    Tagle, D.A.8
  • 199
    • 33845361630 scopus 로고    scopus 로고
    • Motor neuron degeneration in amyotrophic lateral sclerosis mutant superoxide dismutase-1 transgenic mice: Mechanisms of mitochondriopathy and cell death
    • Martin, L. J.; Liu, Z.; Chen, K.; Price, A. C.; Pan, Y.; Swaby, J. A.; Golden, W. C. Motor neuron degeneration in amyotrophic lateral sclerosis mutant superoxide dismutase-1 transgenic mice: mechanisms of mitochondriopathy and cell death. J. Comp. Neurol., 2007, 500(1), 20-46.
    • (2007) J. Comp. Neurol. , vol.500 , Issue.1 , pp. 20-46
    • Martin, L.J.1    Liu, Z.2    Chen, K.3    Price, A.C.4    Pan, Y.5    Swaby, J.A.6    Golden, W.C.7
  • 203
    • 43549117036 scopus 로고    scopus 로고
    • Involvement of dopamine receptors and beta-arrestin in metamphetamine-induced inclusions formation in PC12 cells
    • Fornai, F.; Lenzi, P.; Capobianco, L.; Iacovelli, L.; Scarselli, P.; Lazzeri, G.; De Blasi, A. Involvement of dopamine receptors and beta-arrestin in metamphetamine-induced inclusions formation in PC12 cells. J. Neurochem., 2008, 105(5), 1939-1947.
    • (2008) J. Neurochem. , vol.105 , Issue.5 , pp. 1939-1947
    • Fornai, F.1    Lenzi, P.2    Capobianco, L.3    Iacovelli, L.4    Scarselli, P.5    Lazzeri, G.6    De Blasi, A.7
  • 205
    • 67749133873 scopus 로고    scopus 로고
    • TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity
    • Johnson, B. S.; Snead, D.; Lee, J. J.; McCaffery, J. M.; Shorter, J.; Gitler, A. D. TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. J. Biol. Chem., 2009, 284, 20329-20339.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20329-20339
    • Johnson, B.S.1    Snead, D.2    Lee, J.J.3    McCaffery, J.M.4    Shorter, J.5    Gitler, A.D.6
  • 207
    • 26444471905 scopus 로고    scopus 로고
    • Structural properties and neuronal toxicity of amyotrophic lateral sclerosis-associated Cu/Zn superoxide dismutase 1 aggregates
    • Matsumoto, G.; Stojanovic, A.; Holmberg, C. I.; Kim, S.; Morimoto, R. I. Structural properties and neuronal toxicity of amyotrophic lateral sclerosis-associated Cu/Zn superoxide dismutase 1 aggregates. J. Cell Biol., 2005, 171, 75-85.
    • (2005) J. Cell Biol. , vol.171 , pp. 75-85
    • Matsumoto, G.1    Stojanovic, A.2    Holmberg, C.I.3    Kim, S.4    Morimoto, R.I.5
  • 208
    • 3042817421 scopus 로고    scopus 로고
    • CHIP promotes proteasomal degradation of familial ALS linked mutant SOD1 by ubiquitinating Hsp/Hsc70, J
    • Urushitani, M.; Kurisu, J.; Tateno, M.; Hatakeyama, S.; Nakayama, K.; Kato, S.; Takahashi, R. CHIP promotes proteasomal degradation of familial ALS linked mutant SOD1 by ubiquitinating Hsp/Hsc70, J. Neurochem., 2004, 90, 231-244.
    • (2004) Neurochem. , vol.90 , pp. 231-244
    • Urushitani, M.1    Kurisu, J.2    Tateno, M.3    Hatakeyama, S.4    Nakayama, K.5    Kato, S.6    Takahashi, R.7
  • 209
    • 34247606414 scopus 로고    scopus 로고
    • TDP-43 immunoreactivity in neuronal inclusions in familial amyotrophic lateral sclerosis with or without SOD1 gene mutations
    • Tan, C. F.; Eguchi, H.; Tagawa, A.; Onodera, O.; Iwasaki, T.; Tsujino, A.; Nishizawa, M.; Kakita, A.; Takahashi, H. TDP-43 immunoreactivity in neuronal inclusions in familial amyotrophic lateral sclerosis with or without SOD1 gene mutations. Acta Neuropathol., 2007, 113, 535-542.
    • (2007) Acta Neuropathol. , vol.113 , pp. 535-542
    • Tan, C.F.1    Eguchi, H.2    Tagawa, A.3    Onodera, O.4    Iwasaki, T.5    Tsujino, A.6    Nishizawa, M.7    Kakita, A.8    Takahashi, H.9
  • 212
    • 68749083546 scopus 로고    scopus 로고
    • Variation in aggregation propensities among ALSassociated variants of SOD1: Correlation to human disease
    • Prudencio, M.; Hart, P. J.; Borchelt, D. R.; Andersen, P. M. Variation in aggregation propensities among ALSassociated variants of SOD1: correlation to human disease. Hum. Mol. Genet., 2009, 18, 3217-3226.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 3217-3226
    • Prudencio, M.1    Hart, P.J.2    Borchelt, D.R.3    Andersen, P.M.4
  • 214
    • 77956270117 scopus 로고    scopus 로고
    • Superoxide dismutase 1 and tgSOD1 mouse spinal cord seed fibrils, suggesting a propagative cell death mechanism in amyotrophic lateral sclerosis
    • Chia, R.; Tattum, M. H.; Jones, S.; Collinge, J.; Fisher, E. M.; Jackson, G. S. Superoxide dismutase 1 and tgSOD1 mouse spinal cord seed fibrils, suggesting a propagative cell death mechanism in amyotrophic lateral sclerosis. PLoS One, 2010, 5(5), e10627.
    • (2010) PLoS One , vol.5 , Issue.5 , pp. e10627
    • Chia, R.1    Tattum, M.H.2    Jones, S.3    Collinge, J.4    Fisher, E.M.5    Jackson, G.S.6
  • 215
    • 79952743365 scopus 로고    scopus 로고
    • Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells
    • Munch, C.; O'Brien, J.; Bertolotti, A. Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc. Natl. Acad. Sci. U. S. A., 2011, 108, 3548-3553.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 3548-3553
    • Munch, C.1    O'Brien, J.2    Bertolotti, A.3
  • 218
    • 79955522014 scopus 로고    scopus 로고
    • Autophagy in spinal cord motor neurons in sporadic amyotrophic lateral sclerosis
    • Sasaki, S. Autophagy in spinal cord motor neurons in sporadic amyotrophic lateral sclerosis. J. Neuropathol. Exp. Neurol., 2011, 70(5), 349-359.
    • (2011) J. Neuropathol. Exp. Neurol. , vol.70 , Issue.5 , pp. 349-359
    • Sasaki, S.1
  • 219
    • 47949093588 scopus 로고    scopus 로고
    • Ultrastructural localization of TDP-43 in filamentous neuronal inclusions in various neurodegenerative diseases
    • Lin, W. L.; Dickson, D. W. Ultrastructural localization of TDP-43 in filamentous neuronal inclusions in various neurodegenerative diseases. Acta Neuropathol., 2008, 116, 205-213.
    • (2008) Acta Neuropathol. , vol.116 , pp. 205-213
    • Lin, W.L.1    Dickson, D.W.2
  • 222
    • 84906095611 scopus 로고    scopus 로고
    • Bunina bodies in motor and non-motor neurons revisited: A pathological study of an ALS patient after long-term survival on a respirator
    • in press
    • Kimura, T.; Jiang, H.; Konno, T.; Seto, M.; Iwanaga, K.; Tsujihata, M.; Satoh, A.; Onodera, O.; Kakita, A.; Takahashi, H. Bunina bodies in motor and non-motor neurons revisited: A pathological study of an ALS patient after long-term survival on a respirator. Neuropathology, 2014, in press. doi: 10.1111/neup. 12105.
    • (2014) Neuropathology
    • Kimura, T.1    Jiang, H.2    Konno, T.3    Seto, M.4    Iwanaga, K.5    Tsujihata, M.6    Satoh, A.7    Onodera, O.8    Kakita, A.9    Takahashi, H.10
  • 223
    • 56349119573 scopus 로고    scopus 로고
    • Motor deficit in a Drosophila model of mucolipidosis type IV due to defective clearance of apoptotic cells
    • Venkatachalam, K.; Long, A. A.; Elsaesser, R.; Nikolaeva, D.; Broadie, K.; Montell; C. Motor deficit in a Drosophila model of mucolipidosis type IV due to defective clearance of apoptotic cells. Cell., 2008, 135, 838-851.
    • (2008) Cell. , vol.135 , pp. 838-851
    • Venkatachalam, K.1    Long, A.A.2    Elsaesser, R.3    Nikolaeva, D.4    Broadie, K.5    Montell, C.6
  • 225
    • 33846551867 scopus 로고    scopus 로고
    • The spread of prions through the body in naturally acquired transmissible spongiform encephalopathies
    • Beekes, M.; McBride, P. A. The spread of prions through the body in naturally acquired transmissible spongiform encephalopathies. FEBS J., 2007, 274(3), 588-605.
    • (2007) FEBS J. , vol.274 , Issue.3 , pp. 588-605
    • Beekes, M.1    McBride, P.A.2
  • 226
    • 80052797392 scopus 로고    scopus 로고
    • Transmission of prions within the gut and towards the central nervous system
    • Natale, G.; Ferrucci, M.; Lazzeri, G.; Paparelli, A.; Fornai, F. Transmission of prions within the gut and towards the central nervous system. Prion, 2011, 5(3), 142-149.
    • (2011) Prion , vol.5 , Issue.3 , pp. 142-149
    • Natale, G.1    Ferrucci, M.2    Lazzeri, G.3    Paparelli, A.4    Fornai, F.5
  • 228
    • 77951183978 scopus 로고    scopus 로고
    • Prion-like disorders: Blurring the divide between transmissibility and infectivity
    • Cushman, M.; Johnson, B. S.; King, O. D.; Gitler, A. D.; Shorter, J. Prion-like disorders: blurring the divide between transmissibility and infectivity. J. Cell. Sci., 2010, 123(Pt 8), 1191-1201.
    • (2010) J. Cell. Sci. , vol.123 , pp. 1191-1201
    • Cushman, M.1    Johnson, B.S.2    King, O.D.3    Gitler, A.D.4    Shorter, J.5
  • 229
    • 81855185603 scopus 로고    scopus 로고
    • Parallel manifestations of neuropathologies in the enteric and central nervous systems
    • Natale, G.; Pasquali, L.; Paparelli, A.; Fornai, F. Parallel manifestations of neuropathologies in the enteric and central nervous systems. Neurogastroenterol. Motil., 2011, 23(12), 1056-1065.
    • (2011) Neurogastroenterol. Motil. , vol.23 , Issue.12 , pp. 1056-1065
    • Natale, G.1    Pasquali, L.2    Paparelli, A.3    Fornai, F.4
  • 232
    • 84879033702 scopus 로고    scopus 로고
    • Native α-synuclein induces clustering of synaptic-vesicle mimics via binding to phospholipids and synaptobrevin-2/VAMP2
    • Diao, J.; Burré, J.; Vivona, S.; Cipriano, D. J.; Sharma, M.; Kyoung, M.; Südhof, T. C.; Brunger, A. T. Native α-synuclein induces clustering of synaptic-vesicle mimics via binding to phospholipids and synaptobrevin-2/VAMP2. Elife, 2013, 2:e00592.
    • (2013) Elife , vol.2 , pp. e00592
    • Diao, J.1    Burré, J.2    Vivona, S.3    Cipriano, D.J.4    Sharma, M.5    Kyoung, M.6    Südhof, T.C.7    Brunger, A.T.8
  • 233
    • 79956311051 scopus 로고    scopus 로고
    • A seeding reaction recapitulates intracellular formation of sarkosyl-insoluble TAR DNA binding protein-43 inclusions
    • Furukawa, Y.; Kaneko, K.; Watanabe, S.; Yamanaka, K.; Nukina, N. A seeding reaction recapitulates intracellular formation of sarkosyl-insoluble TAR DNA binding protein-43 inclusions. J. Biol. Chem., 2011, 286(21), 18664-18672.
    • (2011) J. Biol. Chem. , vol.286 , Issue.21 , pp. 18664-18672
    • Furukawa, Y.1    Kaneko, K.2    Watanabe, S.3    Yamanaka, K.4    Nukina, N.5
  • 234
    • 44949216859 scopus 로고    scopus 로고
    • Advanced glycation end-products (AGEs): Involvement in aging and in neurodegenerative diseases
    • Grillo, M. A.; Colombatto, S. Advanced glycation end-products (AGEs): involvement in aging and in neurodegenerative diseases. Amino Acids., 2008, 35(1), 29-36.
    • (2008) Amino Acids. , vol.35 , Issue.1 , pp. 29-36
    • Grillo, M.A.1    Colombatto, S.2
  • 235
    • 0031876839 scopus 로고    scopus 로고
    • Advanced glycation endproducts in neurofilament conglomeration of motoneurons in familial and sporadic amyotrophic lateral sclerosis
    • Chou, S. M.; Wang, H. S.; Taniguchi, A.; Bucala, R. Advanced glycation endproducts in neurofilament conglomeration of motoneurons in familial and sporadic amyotrophic lateral sclerosis. Mol. Med., 1998, 4(5), 324-332.
    • (1998) Mol. Med. , vol.4 , Issue.5 , pp. 324-332
    • Chou, S.M.1    Wang, H.S.2    Taniguchi, A.3    Bucala, R.4
  • 237
    • 0035992927 scopus 로고    scopus 로고
    • Detection of N epsilon-(carboxymethyl) lysine (CML) and non-CML advanced glycation end-products in the anterior horn of amyotrophic lateral sclerosis spinal cord
    • Kikuchi, S.; Shinpo, K.; Ogata, A.; Tsuji, S.; Takeuchi, M.; Makita, Z.; Tashiro, K. Detection of N epsilon-(carboxymethyl) lysine (CML) and non-CML advanced glycation end-products in the anterior horn of amyotrophic lateral sclerosis spinal cord. Amyotroph. Lateral Scler. Other Motor Neuron. Disord., 2002, 3(2), 63-68.
    • (2002) Amyotroph. Lateral Scler. Other Motor Neuron. Disord. , vol.3 , Issue.2 , pp. 63-68
    • Kikuchi, S.1    Shinpo, K.2    Ogata, A.3    Tsuji, S.4    Takeuchi, M.5    Makita, Z.6    Tashiro, K.7
  • 238
    • 0032980525 scopus 로고    scopus 로고
    • Advanced glycation endproducts are deposited in neuronal hyaline inclusions: A study on familial amyotrophic lateral sclerosis with superoxide dismutase-1 mutation
    • Shibata, N.; Hirano, A.; Kato, S.; Nagai, R.; Horiuchi, S.; Komori, T.; Umahara, T.; Asayama, K.; Kobayashi, M. Advanced glycation endproducts are deposited in neuronal hyaline inclusions: a study on familial amyotrophic lateral sclerosis with superoxide dismutase-1 mutation. Acta Neuropathol., 1999;97(3), 240-246.
    • (1999) Acta Neuropathol. , vol.97 , Issue.3 , pp. 240-246
    • Shibata, N.1    Hirano, A.2    Kato, S.3    Nagai, R.4    Horiuchi, S.5    Komori, T.6    Umahara, T.7    Asayama, K.8    Kobayashi, M.9
  • 240
    • 0033823740 scopus 로고    scopus 로고
    • Advanced glycation endproduct-modified superoxide dismutase-1 (SOD1)-positive inclusions are common to familial amyotrophic lateral sclerosis patients with SOD1 gene mutations and transgenic mice expressing human SOD1 with a G85R mutation
    • Kato, S.; Horiuchi, S.; Liu, J.; Cleveland, D. W.; Shibata, N.; Nakashima, K.; Nagai, R.; Hirano, A.; Takikawa, M.; Kato, M.; Nakano, I.; Ohama, E. Advanced glycation endproduct-modified superoxide dismutase-1 (SOD1)-positive inclusions are common to familial amyotrophic lateral sclerosis patients with SOD1 gene mutations and transgenic mice expressing human SOD1 with a G85R mutation. Acta Neuropathol., 2000, 100(5), 490-505.
    • (2000) Acta Neuropathol. , vol.100 , Issue.5 , pp. 490-505
    • Kato, S.1    Horiuchi, S.2    Liu, J.3    Cleveland, D.W.4    Shibata, N.5    Nakashima, K.6    Nagai, R.7    Hirano, A.8    Takikawa, M.9    Kato, M.10    Nakano, I.11    Ohama, E.12
  • 241
    • 0034209203 scopus 로고    scopus 로고
    • New consensus research on neuropathological aspects of familial amyotrophic lateral sclerosis with superoxide dismutase 1 (SOD1) gene mutations: Inclusions containing SOD1 in neurons and astrocytes
    • Kato, S.; Takikawa, M.; Nakashima, K.; Hirano, A.; Cleveland, D. W.; Kusaka, H.; Shibata, N.; Kato, M.; Nakano, I.; Ohama, E. New consensus research on neuropathological aspects of familial amyotrophic lateral sclerosis with superoxide dismutase 1 (SOD1) gene mutations: inclusions containing SOD1 in neurons and astrocytes. Amyotroph. Lateral Scler. Other Motor Neuron. Disord., 2000, 1(3), 163-184
    • (2000) Amyotroph. Lateral Scler. Other Motor Neuron. Disord. , vol.1 , Issue.3 , pp. 163-184
    • Kato, S.1    Takikawa, M.2    Nakashima, K.3    Hirano, A.4    Cleveland, D.W.5    Kusaka, H.6    Shibata, N.7    Kato, M.8    Nakano, I.9    Ohama, E.10
  • 242
    • 39749162770 scopus 로고    scopus 로고
    • The role of exosomes in the processing of proteins associated with neurodegenerative diseases
    • Vella, L. J.; Sharples, R. A.; Nisbet, R. M.; Cappai, R.; Hill, A. F. The role of exosomes in the processing of proteins associated with neurodegenerative diseases. Eur. Biophys. J., 2008, 37, 323-332.
    • (2008) Eur. Biophys. J. , vol.37 , pp. 323-332
    • Vella, L.J.1    Sharples, R.A.2    Nisbet, R.M.3    Cappai, R.4    Hill, A.F.5
  • 245
    • 57249089081 scopus 로고    scopus 로고
    • Immunolocalisation of PrPSc in scrapie-infected N2a mouse neuroblastoma cells by light and electron microscopy
    • Veith, N. M.; Plattner, H.; Stuermer, C. A.; Schulz-Schaeffer, W. J.; Bürkle, A. Immunolocalisation of PrPSc in scrapie-infected N2a mouse neuroblastoma cells by light and electron microscopy. Eur. J. Cell. Biol., 2009, 88(1), 45-63.
    • (2009) Eur. J. Cell. Biol. , vol.88 , Issue.1 , pp. 45-63
    • Veith, N.M.1    Plattner, H.2    Stuermer, C.A.3    Schulz-Schaeffer, W.J.4    Bürkle, A.5
  • 246
    • 35448956015 scopus 로고    scopus 로고
    • Evidence for secretion of Cu, Zn superoxide dismutase via exosomes from a cell model of amyotrophic lateral sclerosis
    • Gomes, C.; Keller, S.; Altevogt, P.; Costa J. Evidence for secretion of Cu, Zn superoxide dismutase via exosomes from a cell model of amyotrophic lateral sclerosis. Neurosci. Lett., 2007, 428(1), 43-46.
    • (2007) Neurosci. Lett. , vol.428 , Issue.1 , pp. 43-46
    • Gomes, C.1    Keller, S.2    Altevogt, P.3    Costa, J.4
  • 247
    • 84878389217 scopus 로고    scopus 로고
    • Mutant copper-zinc superoxide dismutase (SOD1) induces protein secretion pathway alterations and exosome release in astrocytes: Implications for disease spreading and motor neuron pathology in amyotrophic lateral sclerosis
    • Basso, M.; Pozzi, S.; Tortarolo, M.; Fiordaliso, F.; Bisighini, C.; Pasetto, L.; Spaltro, G.; Lidonnici, D.; Gensano, F.; Battaglia, E.; Bendotti, C.; Bonetto, V. Mutant copper-zinc superoxide dismutase (SOD1) induces protein secretion pathway alterations and exosome release in astrocytes: implications for disease spreading and motor neuron pathology in amyotrophic lateral sclerosis. J. Biol. Chem., 2013, 288(22), 15699-15711.
    • (2013) J. Biol. Chem. , vol.288 , Issue.22 , pp. 15699-15711
    • Basso, M.1    Pozzi, S.2    Tortarolo, M.3    Fiordaliso, F.4    Bisighini, C.5    Pasetto, L.6    Spaltro, G.7    Lidonnici, D.8    Gensano, F.9    Battaglia, E.10    Bendotti, C.11    Bonetto, V.12
  • 249
    • 84871118236 scopus 로고    scopus 로고
    • The exosome secretory pathway transports amyloid precursor protein carboxyl-terminal fragments from the cell into the brain extracellular space
    • Perez-Gonzalez, R.; Gauthier, S. A.; Kumar, A.; Levy, E. The exosome secretory pathway transports amyloid precursor protein carboxyl-terminal fragments from the cell into the brain extracellular space. J. Biol. Chem., 2012, 287(51), 43108-43115.
    • (2012) J. Biol. Chem. , vol.287 , Issue.51 , pp. 43108-43115
    • Perez-Gonzalez, R.1    Gauthier, S.A.2    Kumar, A.3    Levy, E.4
  • 252
    • 84880135337 scopus 로고    scopus 로고
    • Exosomes of BV-2 cells induced by alpha-synuclein: Important mediator of neurodegeneration in PD
    • Chang, C.; Lang, H.; Geng, N.; Wang, J.; Li, N.; Wang X. Exosomes of BV-2 cells induced by alpha-synuclein: important mediator of neurodegeneration in PD. Neurosci. Lett., 2013, 548, 190-195.
    • (2013) Neurosci. Lett. , vol.548 , pp. 190-195
    • Chang, C.1    Lang, H.2    Geng, N.3    Wang, J.4    Li, N.5    Wang, X.6
  • 253
    • 0034840664 scopus 로고    scopus 로고
    • Involvement of microglial receptor for advanced glycation endproducts (RAGE) in Alzheimer's disease: Identification of a cellular activation mechanism
    • Lue, L. F.; Walker, D. G.; Brachova, L.; Beach, T. G.; Rogers, J.; Schmidt, A. M.; Stern, D. M.; Yan, S. D. Involvement of microglial receptor for advanced glycation endproducts (RAGE) in Alzheimer's disease: identification of a cellular activation mechanism. Exp. Neurol., 2001, 171(1), 29-45.
    • (2001) Exp. Neurol. , vol.171 , Issue.1 , pp. 29-45
    • Lue, L.F.1    Walker, D.G.2    Brachova, L.3    Beach, T.G.4    Rogers, J.5    Schmidt, A.M.6    Stern, D.M.7    Yan, S.D.8
  • 254
    • 0035847269 scopus 로고    scopus 로고
    • Immunohistochemical distribution of the receptor for advanced glycation end products in neurons and astrocytes in Alzheimer's disease
    • Sasaki, N.; Toki, S.; Chowei, H.; Saito, T.; Nakano, N.; Hayashi, Y.; Takeuchi, M.; Makita, Z. Immunohistochemical distribution of the receptor for advanced glycation end products in neurons and astrocytes in Alzheimer's disease. Brain Res., 2001, 888(2), 256-262.
    • (2001) Brain Res. , vol.888 , Issue.2 , pp. 256-262
    • Sasaki, N.1    Toki, S.2    Chowei, H.3    Saito, T.4    Nakano, N.5    Hayashi, Y.6    Takeuchi, M.7    Makita, Z.8
  • 255
    • 84865647121 scopus 로고    scopus 로고
    • The diverse ligand repertoire of the receptor for advanced glycation endproducts and pathways to the complications of diabetes
    • Ramasamy, R.; Yan, S. F.; Schmidt, A. M. The diverse ligand repertoire of the receptor for advanced glycation endproducts and pathways to the complications of diabetes. Vascul. Pharmacol., 2012, 57(5-6), 160-167.
    • (2012) Vascul. Pharmacol. , vol.57 , Issue.5-6 , pp. 160-167
    • Ramasamy, R.1    Yan, S.F.2    Schmidt, A.M.3
  • 256
    • 84864885117 scopus 로고    scopus 로고
    • Receptor for advanced glycation end products (RAGE) and implications for the pathophysiology of heart failure
    • Ramasamy, R.; Schmidt, A. M. Receptor for advanced glycation end products (RAGE) and implications for the pathophysiology of heart failure. Curr. Heart. Fail. Rep., 2012, 9(2), 107-116.
    • (2012) Curr. Heart. Fail. Rep. , vol.9 , Issue.2 , pp. 107-116
    • Ramasamy, R.1    Schmidt, A.M.2
  • 258
    • 78649994498 scopus 로고    scopus 로고
    • Blockade of PKC-beta protects HUVEC from advanced glycation end products induced inflammation
    • Xu, Y.; Wang, S.; Feng, L.; Zhu, Q.; Xiang, P.; He, B. Blockade of PKC-beta protects HUVEC from advanced glycation end products induced inflammation. Int. Immunopharmacol., 2010, 10(12), 1552-1559.
    • (2010) Int. Immunopharmacol. , vol.10 , Issue.12 , pp. 1552-1559
    • Xu, Y.1    Wang, S.2    Feng, L.3    Zhu, Q.4    Xiang, P.5    He, B.6
  • 259
    • 84883348572 scopus 로고    scopus 로고
    • Transfer of polyglutamine aggregates in neuronal cells occurs in tunneling nanotubes
    • Costanzo, M.; Abounit, S.; Marzo, L.; Danckaert, A.; Chamoun, Z.; Roux, P.; Zurzolo, C. Transfer of polyglutamine aggregates in neuronal cells occurs in tunneling nanotubes. J. Cell Sci., 2013, 126(Pt 16), 3678-3685.
    • (2013) J. Cell Sci. , vol.126 , pp. 3678-3685
    • Costanzo, M.1    Abounit, S.2    Marzo, L.3    Danckaert, A.4    Chamoun, Z.5    Roux, P.6    Zurzolo, C.7
  • 261
    • 70349561098 scopus 로고    scopus 로고
    • Tunnelling nanotubes: A highway for prion spreading?
    • Gousset, K.; Zurzolo, C. Tunnelling nanotubes: a highway for prion spreading? Prion, 2009, 3(2), 94-98.
    • (2009) Prion , vol.3 , Issue.2 , pp. 94-98
    • Gousset, K.1    Zurzolo, C.2
  • 262
    • 84866327994 scopus 로고    scopus 로고
    • Multifaceted roles of tunneling nanotubes in intercellular communication
    • Marzo, L.; Gousset, K.; Zurzolo, C. Multifaceted roles of tunneling nanotubes in intercellular communication. Front. Physiol., 2012, 3, 72.
    • (2012) Front. Physiol. , vol.3 , pp. 72
    • Marzo, L.1    Gousset, K.2    Zurzolo, C.3
  • 263
    • 33646558563 scopus 로고    scopus 로고
    • Molecular morphology and toxicity of cytoplasmic prion protein aggregates in neuronal and non-neuronal cells
    • Grenier, C.; Bissonnette, C.; Volkov, L.; Roucou, X. Molecular morphology and toxicity of cytoplasmic prion protein aggregates in neuronal and non-neuronal cells. J. Neurochem., 2006, 97(5), 1456-1466.
    • (2006) J. Neurochem. , vol.97 , Issue.5 , pp. 1456-1466
    • Grenier, C.1    Bissonnette, C.2    Volkov, L.3    Roucou, X.4
  • 264
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston, J. A.; Ward, C. L.; Kopito, R. R. Aggresomes: a cellular response to misfolded proteins. J. Cell. Biol., 1998, 143(7):1883-1898.
    • (1998) J. Cell. Biol. , vol.143 , Issue.7 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 265
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito, R. R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell. Biol., 2000, 10(12), 524-530.
    • (2000) Trends Cell. Biol. , vol.10 , Issue.12 , pp. 524-530
    • Kopito, R.R.1
  • 267
    • 79959385443 scopus 로고    scopus 로고
    • Mechanisms of cellular communication through intercellular protein transfer
    • Ahmed, K. A.; Xiang, J. Mechanisms of cellular communication through intercellular protein transfer. J. Cell. Mol. Med., 2011, 15(7), 1458-1473.
    • (2011) J. Cell. Mol. Med. , vol.15 , Issue.7 , pp. 1458-1473
    • Ahmed, K.A.1    Xiang, J.2
  • 268
    • 84877342306 scopus 로고    scopus 로고
    • Cell biology. Unconventional secretion, unconventional solutions
    • Zhang, M.; Schekman, R. Cell biology. Unconventional secretion, unconventional solutions. Science, 2013, 340(6132), 559-561.
    • (2013) Science , vol.340 , Issue.6132 , pp. 559-561
    • Zhang, M.1    Schekman, R.2
  • 269
    • 0035132167 scopus 로고    scopus 로고
    • Increased expression of the pro-inflammatory enzyme cyclooxygenase-2 in amyotrophic lateral sclerosis
    • Almer, G.; Guégan, C.; Teismann, P.; Naini, A.; Rosoklija, G.; Hays, A. P.; Chen, C.; Przedborski, S. Increased expression of the pro-inflammatory enzyme cyclooxygenase-2 in amyotrophic lateral sclerosis. Ann. Neurol., 2001, 49(2), 176-185.
    • (2001) Ann. Neurol. , vol.49 , Issue.2 , pp. 176-185
    • Almer, G.1    Guégan, C.2    Teismann, P.3    Naini, A.4    Rosoklija, G.5    Hays, A.P.6    Chen, C.7    Przedborski, S.8
  • 270
    • 0036787810 scopus 로고    scopus 로고
    • Inflammatory processes in amyotrophic lateral sclerosis
    • McGeer, P. L.; McGeer, E. G. Inflammatory processes in amyotrophic lateral sclerosis. Muscle Nerve, 2002, 26(4), 459-470.
    • (2002) Muscle Nerve , vol.26 , Issue.4 , pp. 459-470
    • McGeer, P.L.1    McGeer, E.G.2
  • 271
    • 77955506963 scopus 로고    scopus 로고
    • Appearance of phagocytic microglia adjacent to motoneurons in spinal cord tissue from a presymptomatic transgenic rat model of amyotrophic lateral sclerosis
    • Sanagi, T.; Yuasa, S.; Nakamura, Y.; Suzuki, E.; Aoki, M.; Warita, H.; Itoyama, Y.; Uchino, S.; Kohsaka, S.; Ohsawa, K. Appearance of phagocytic microglia adjacent to motoneurons in spinal cord tissue from a presymptomatic transgenic rat model of amyotrophic lateral sclerosis. J. Neurosci. Res., 2010, 88(12), 2736-2746.
    • (2010) J. Neurosci. Res. , vol.88 , Issue.12 , pp. 2736-2746
    • Sanagi, T.1    Yuasa, S.2    Nakamura, Y.3    Suzuki, E.4    Aoki, M.5    Warita, H.6    Itoyama, Y.7    Uchino, S.8    Kohsaka, S.9    Ohsawa, K.10
  • 272
    • 79951704433 scopus 로고    scopus 로고
    • Neuroinflammation in amyotrophic lateral sclerosis: Role of glial activation in motor neuron disease
    • Philips, T.; Robberecht, W. Neuroinflammation in amyotrophic lateral sclerosis: role of glial activation in motor neuron disease. Lancet Neurol., 2011, 10(3), 253-263.
    • (2011) Lancet Neurol. , vol.10 , Issue.3 , pp. 253-263
    • Philips, T.1    Robberecht, W.2
  • 276
    • 79957927732 scopus 로고    scopus 로고
    • Neuroinflammation modulates distinct regional and temporal clinical responses in ALS mice
    • Beers, D. R.; Zhao, W.; Liao, B.; Kano, O.; Wang, J.; Huang, A.; Appel, S. H.; Henkel, J. S. Neuroinflammation modulates distinct regional and temporal clinical responses in ALS mice. Brain Behav. Immun., 2011, 25(5), 1025-1035.
    • (2011) Brain Behav. Immun. , vol.25 , Issue.5 , pp. 1025-1035
    • Beers, D.R.1    Zhao, W.2    Liao, B.3    Kano, O.4    Wang, J.5    Huang, A.6    Appel, S.H.7    Henkel, J.S.8
  • 279
    • 0032472831 scopus 로고    scopus 로고
    • Time course of neuropathology in the spinal cord of G86R superoxide dismutase transgenic mice
    • Morrison, B. M.; Janssen, W. G.; Gordon, J. W.; Morrison, J. H. Time course of neuropathology in the spinal cord of G86R superoxide dismutase transgenic mice. J. Comp. Neurol., 1998, 391(1), 64-77.
    • (1998) J. Comp. Neurol. , vol.391 , Issue.1 , pp. 64-77
    • Morrison, B.M.1    Janssen, W.G.2    Gordon, J.W.3    Morrison, J.H.4
  • 280
    • 59649104173 scopus 로고    scopus 로고
    • Glycinergic innervation of motoneurons is deficient in amyotrophic lateral sclerosis mice: A quantitative confocal analysis
    • Chang, Q.; Martin, L. J. Glycinergic innervation of motoneurons is deficient in amyotrophic lateral sclerosis mice: a quantitative confocal analysis. Am. J. Pathol., 2009, 174(2), 574-585.
    • (2009) Am. J. Pathol. , vol.174 , Issue.2 , pp. 574-585
    • Chang, Q.1    Martin, L.J.2
  • 281
    • 33646082251 scopus 로고    scopus 로고
    • Widespread loss of neuronal populations in the spinal ventral horn in sporadic motor neuron disease. A morphometric study
    • Stephens B, Guiloff RJ, Navarrete R, Newman P, Nikhar N, Lewis P. Widespread loss of neuronal populations in the spinal ventral horn in sporadic motor neuron disease. A morphometric study. J. Neurol Sci., 2006, 244, 41-58.
    • (2006) J. Neurol Sci. , vol.244 , pp. 41-58
    • Stephens, B.1    Guiloff, R.J.2    Navarrete, R.3    Newman, P.4    Nikhar, N.5    Lewis, P.6
  • 283
    • 74149092630 scopus 로고    scopus 로고
    • Lithium prevents excitotoxic cell death of motoneurons in organotypic slice cultures of spinal cord
    • Calderó, J.; Brunet, N.; Tarabal, O.; Piedrafita, L.; Hereu, M.; Ayala, V.; Esquerda, J. E. Lithium prevents excitotoxic cell death of motoneurons in organotypic slice cultures of spinal cord. Neuroscience, 2010, 165(4), 1353-1369.
    • (2010) Neuroscience , vol.165 , Issue.4 , pp. 1353-1369
    • Calderó, J.1    Brunet, N.2    Tarabal, O.3    Piedrafita, L.4    Hereu, M.5    Ayala, V.6    Esquerda, J.E.7
  • 285
    • 79953647105 scopus 로고    scopus 로고
    • Rapamycin treatment augments motor neuron degeneration in SOD1 (G93A) mouse model of amyotrophic lateral sclerosis
    • Zhang, X.; Li, L.; Chen, S.; Yang, D.; Wang, Y.; Zhang, X.; Wang, Z.; Le, W. Rapamycin treatment augments motor neuron degeneration in SOD1 (G93A) mouse model of amyotrophic lateral sclerosis. Autophagy, 2011, 7(4), 412-425.
    • (2011) Autophagy , vol.7 , Issue.4 , pp. 412-425
    • Zhang, X.1    Li, L.2    Chen, S.3    Yang, D.4    Wang, Y.5    Zhang, X.6    Wang, Z.7    Le, W.8
  • 286
    • 84878758681 scopus 로고    scopus 로고
    • Food restriction-induced autophagy modulates degradation of mutant SOD1 in an amyotrophic lateral sclerosis mouse model
    • Zhang, K.; Shi, P.; An, T.; Wang, Q.; Wang, J.; Li, Z.; Duan, W.; Li, C.; Guo, Y. Food restriction-induced autophagy modulates degradation of mutant SOD1 in an amyotrophic lateral sclerosis mouse model. Brain Res., 2013, 1519, 112-119.
    • (2013) Brain Res. , vol.1519 , pp. 112-119
    • Zhang, K.1    Shi, P.2    An, T.3    Wang, Q.4    Wang, J.5    Li, Z.6    Duan, W.7    Li, C.8    Guo, Y.9
  • 287
    • 84872740046 scopus 로고    scopus 로고
    • Therapeutic effects of valproate combined with lithium carbonate on MPTP-induced parkinsonism in mice: Possible mediation through enhanced autophagy
    • Li, X. Z.; Chen, X. P.; Zhao, K.; Bai, L. M.; Zhang, H.; Zhou, X. P. Therapeutic effects of valproate combined with lithium carbonate on MPTP-induced parkinsonism in mice: possible mediation through enhanced autophagy. Int. J. Neurosci., 2013, 123(2), 73-79.
    • (2013) Int. J. Neurosci. , vol.123 , Issue.2 , pp. 73-79
    • Li, X.Z.1    Chen, X.P.2    Zhao, K.3    Bai, L.M.4    Zhang, H.5    Zhou, X.P.6
  • 289
    • 84894355071 scopus 로고    scopus 로고
    • Lithium Down-regulates Histone Deacetylase 1 (HDAC1) and induces degradation of mutant huntingtin
    • Wu, S.; Zheng, S. D.; Huang, H. L.; Yan, L. C.; Yin, X. F.; Xu, H. N.; Zhang, K. J.; Gui, J. H.; Chu, L.; Liu, X. Y. Lithium Down-regulates Histone Deacetylase 1 (HDAC1) and Induces Degradation of Mutant Huntingtin. J. Biol. Chem., 2013, 288(49), 35500-35510.
    • (2013) J. Biol. Chem. , vol.288 , Issue.49 , pp. 35500-35510
    • Wu, S.1    Zheng, S.D.2    Huang, H.L.3    Yan, L.C.4    Yin, X.F.5    Xu, H.N.6    Zhang, K.J.7    Gui, J.H.8    Chu, L.9    Liu, X.Y.10
  • 290
    • 77950628380 scopus 로고    scopus 로고
    • Northeast and Canadian Amyotrophic Lateral Sclerosis consortia. Safety and efficacy of lithium in combination with riluzole for treatment of amyotrophic lateral sclerosis: A randomised, double-blind, placebo-controlled trial
    • Aggarwal, S. P.; Zinman, L.; Simpson, E.; McKinley, J.; Jackson, K. E.; Pinto, H.; Kaufman, P.; Conwit, R. A.; Schoenfeld, D.; Shefner, J.; Cudkowicz, M.; Northeast and Canadian Amyotrophic Lateral Sclerosis consortia. Safety and efficacy of lithium in combination with riluzole for treatment of amyotrophic lateral sclerosis: a randomised, double-blind, placebo-controlled trial. Lancet Neurol., 2010, 9(5), 481-488.
    • (2010) Lancet Neurol. , vol.9 , Issue.5 , pp. 481-488
    • Aggarwal, S.P.1    Zinman, L.2    Simpson, E.3    McKinley, J.4    Jackson, K.E.5    Pinto, H.6    Kaufman, P.7    Conwit, R.A.8    Schoenfeld, D.9    Shefner, J.10    Cudkowicz, M.11
  • 294
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein
    • Sarkar, S.; Davies, J. E.; Huang, Z.; Tunnacliffe, A.; Rubinsztein, D. C. Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein. J. Biol. Chem., 2007, 282(8), 5641-5652.
    • (2007) J. Biol. Chem. , vol.282 , Issue.8 , pp. 5641-5652
    • Sarkar, S.1    Davies, J.E.2    Huang, Z.3    Tunnacliffe, A.4    Rubinsztein, D.C.5
  • 297
    • 23944465642 scopus 로고    scopus 로고
    • 2+, mitochondria and selective motoneuron vulnerability: Implications for ALS
    • 2+, mitochondria and selective motoneuron vulnerability: implications for ALS. Trends Neurosci., 2005, 28, 494-500.
    • (2005) Trends Neurosci. , vol.28 , pp. 494-500
    • Von Lewinski, F.1    Keller, B.U.2
  • 298
    • 84898465382 scopus 로고    scopus 로고
    • MTOR-independent, autophagic enhancer trehalose prolongs motor neuron survival and ameliorates the autophagic flux defect in a mouse model of amyotrophic lateral sclerosis
    • Zhang, X.; Chen, S.; Song, L.; Tang, Y.; Shen, Y.; Jia, L.; Le, W. MTOR-independent, autophagic enhancer trehalose prolongs motor neuron survival and ameliorates the autophagic flux defect in a mouse model of amyotrophic lateral sclerosis. Autophagy, 2014, 10, 22-36.
    • (2014) Autophagy , vol.10 , pp. 22-36
    • Zhang, X.1    Chen, S.2    Song, L.3    Tang, Y.4    Shen, Y.5    Jia, L.6    Le, W.7
  • 302
    • 67649811029 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore in motor neurons: Involvement in the pathobiology of ALS mice
    • Martin, L. J.; Gertz, B.; Pan, Y.; Price, A. C.; Molkentin, J. D.; Chang, Q. The mitochondrial permeability transition pore in motor neurons: involvement in the pathobiology of ALS mice. Exp. Neurol., 2009, 218(2), 333-346.
    • (2009) Exp. Neurol. , vol.218 , Issue.2 , pp. 333-346
    • Martin, L.J.1    Gertz, B.2    Pan, Y.3    Price, A.C.4    Molkentin, J.D.5    Chang, Q.6
  • 303
    • 77956183828 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and intracellular calcium dysregulation in ALS
    • Kawamata, H.; Manfredi, G. Mitochondrial dysfunction and intracellular calcium dysregulation in ALS. Mech. Ageing Dev., 2010, 131, 517-526.
    • (2010) Mech. Ageing Dev. , vol.131 , pp. 517-526
    • Kawamata, H.1    Manfredi, G.2
  • 304
    • 84857061515 scopus 로고    scopus 로고
    • Mitochondrial pathobiology in ALS
    • Martin, L. J. Mitochondrial pathobiology in ALS. J. Bioenerg. Biomembr., 2011, 43(6), 569-579.
    • (2011) J. Bioenerg. Biomembr. , vol.43 , Issue.6 , pp. 569-579
    • Martin, L.J.1
  • 305
    • 83455217437 scopus 로고    scopus 로고
    • Ultrastructural mitochondrial abnormalities in patients with sporadic amyotrophic lateral sclerosis
    • Napoli, L.; Crugnola, V.; Lamperti, C.; Silani, V.; Di Mauro, S.; Bresolin, N.; Moggio, M. Ultrastructural mitochondrial abnormalities in patients with sporadic amyotrophic lateral sclerosis. Arch. Neurol., 2011, 68(12), 1612-1613.
    • (2011) Arch. Neurol. , vol.68 , Issue.12 , pp. 1612-1613
    • Napoli, L.1    Crugnola, V.2    Lamperti, C.3    Silani, V.4    Di Mauro, S.5    Bresolin, N.6    Moggio, M.7
  • 306
    • 0038446768 scopus 로고    scopus 로고
    • Reduction of oxidative stress in amyotrophic lateral sclerosis following pramipexole treatment. Amyotroph. Lateral Scler
    • Pattee, G. L.; Post, G. R.; Gerber, R. E.; Bennett, J. P. Jr. Reduction of oxidative stress in amyotrophic lateral sclerosis following pramipexole treatment. Amyotroph. Lateral Scler. Other Motor Neuron. Disord., 2003, 4(2), 90-95.
    • (2003) Other Motor Neuron. Disord. , vol.4 , Issue.2 , pp. 90-95
    • Pattee, G.L.1    Post, G.R.2    Gerber, R.E.3    Bennett, J.P.4
  • 308
    • 79952753921 scopus 로고    scopus 로고
    • Safety, tolerability, and pharmacokinetics of KNS-760704 (dexpramipexole) in healthy adult subjects
    • Bozik, M. E.; Mather, J. L.; Kramer, W. G.; Gribkoff, V. K.; Ingersoll, E. W. Safety, tolerability, and pharmacokinetics of KNS-760704 (dexpramipexole) in healthy adult subjects. J. Clin. Pharmacol., 2011, 51(8), 1177-1185.
    • (2011) J. Clin. Pharmacol. , vol.51 , Issue.8 , pp. 1177-1185
    • Bozik, M.E.1    Mather, J.L.2    Kramer, W.G.3    Gribkoff, V.K.4    Ingersoll, E.W.5
  • 310
    • 84875428371 scopus 로고    scopus 로고
    • Dexpramipexole effects on functional decline and survival in subjects with amyotrophic lateral sclerosis in a Phase II study: Subgroup analysis of demographic and clinical characteristics
    • Rudnicki, S. A.; Berry, J. D.; Ingersoll, E.; Archibald, D.; Cudkowicz, M. E.; Kerr, D. A.; Dong, Y. Dexpramipexole effects on functional decline and survival in subjects with amyotrophic lateral sclerosis in a Phase II study: subgroup analysis of demographic and clinical characteristics. Amyotroph. Lateral Scler. Frontotemporal Degener., 2013, 14(1), 44-51.
    • (2013) Amyotroph. Lateral Scler. Frontotemporal Degener. , vol.14 , Issue.1 , pp. 44-51
    • Rudnicki, S.A.1    Berry, J.D.2    Ingersoll, E.3    Archibald, D.4    Cudkowicz, M.E.5    Kerr, D.A.6    Dong, Y.7
  • 312
    • 85039891578 scopus 로고    scopus 로고
    • Biogen Idec. http://www.medscape.com/viewarticle/777141.
    • Biogen Idec1
  • 313
    • 84874914445 scopus 로고    scopus 로고
    • Enhancing mitochondrial calcium buffering capacity reduces aggregation of misfolded SOD1 and motor neuron cell death without extending survival in mouse models of inherited amyotrophic lateral sclerosis
    • Parone, P. A.; Da Cruz, S.; Han, J. S.; McAlonis-Downes, M.; Vetto, A. P.; Lee, S. K.; Tseng, E.; Cleveland, D. W. Enhancing mitochondrial calcium buffering capacity reduces aggregation of misfolded SOD1 and motor neuron cell death without extending survival in mouse models of inherited amyotrophic lateral sclerosis. J. Neurosci., 2013, 33(11), 4657-4671.
    • (2013) J. Neurosci. , vol.33 , Issue.11 , pp. 4657-4671
    • Parone, P.A.1    Da Cruz, S.2    Han, J.S.3    McAlonis-Downes, M.4    Vetto, A.P.5    Lee, S.K.6    Tseng, E.7    Cleveland, D.W.8
  • 314
    • 79952325543 scopus 로고    scopus 로고
    • Endosomal accumulation of APP in wobbler motor neurons reflects impaired vesicle trafficking: Implications for human motor neuron disease
    • Palmisano, R.; Golfi, P.; Heimann, P.; Shaw, C.; Troakes, C.; Schmitt-John, T.; Bartsch, J. W. Endosomal accumulation of APP in wobbler motor neurons reflects impaired vesicle trafficking: implications for human motor neuron disease. B. M. C. Neurosci., 2011, 12, 24.
    • (2011) B. M. C. Neurosci. , vol.12 , pp. 24
    • Palmisano, R.1    Golfi, P.2    Heimann, P.3    Shaw, C.4    Troakes, C.5    Schmitt-John, T.6    Bartsch, J.W.7
  • 315
    • 0023256657 scopus 로고
    • Recent views on amyotrophic lateral sclerosis with emphasis on electrophysiological studies
    • Bradley, W. G. Recent views on amyotrophic lateral sclerosis with emphasis on electrophysiological studies. Muscle Nerve, 1987, 10(6), 490-502.
    • (1987) Muscle Nerve , vol.10 , Issue.6 , pp. 490-502
    • Bradley, W.G.1
  • 316
    • 0030847994 scopus 로고    scopus 로고
    • Functional properties of motor units in motor neuron diseases and neuropathies
    • Vogt, T.; Nix, W. A. Functional properties of motor units in motor neuron diseases and neuropathies. Electroencephalogr. Clin. Neurophysiol., 1997, 105(4), 328-332.
    • (1997) Electroencephalogr. Clin. Neurophysiol. , vol.105 , Issue.4 , pp. 328-332
    • Vogt, T.1    Nix, W.A.2
  • 317
    • 84878839731 scopus 로고    scopus 로고
    • Candidate ALS therapeutics motor toward "in vitro clinical trials"
    • Kim, Y. J.; Lee, G. Candidate ALS therapeutics motor toward "in vitro clinical trials". Cell Stem Cell, 2013, 12(6), 633-634.
    • (2013) Cell Stem Cell , vol.12 , Issue.6 , pp. 633-634
    • Kim, Y.J.1    Lee, G.2
  • 318
    • 84891836716 scopus 로고    scopus 로고
    • Intraspinal stem cell transplantation in amyotrophic lateral sclerosis: A phase I trial, cervical microinjection, and final surgical safety outcomes
    • Riley, J.; Glass, J.; Feldman, E. L.; Polak, M.; Bordeau, J.; Federici, T.; Johe, K.; Boulis, N. M. Intraspinal stem cell transplantation in amyotrophic lateral sclerosis: a phase I trial, cervical microinjection, and final surgical safety outcomes. Neurosurgery, 2014, 74(1), 77-87.
    • (2014) Neurosurgery , vol.74 , Issue.1 , pp. 77-87
    • Riley, J.1    Glass, J.2    Feldman, E.L.3    Polak, M.4    Bordeau, J.5    Federici, T.6    Johe, K.7    Boulis, N.M.8
  • 320
    • 79952827651 scopus 로고    scopus 로고
    • Future therapeutical strategies dictated by pre-clinical evidence in ALS
    • Fornai, F.; Meninger, V.; Silani, V. Future therapeutical strategies dictated by pre-clinical evidence in ALS. Arch. Ital. Biol., 2011, 149(1), 169-174.
    • (2011) Arch. Ital. Biol. , vol.149 , Issue.1 , pp. 169-174
    • Fornai, F.1    Meninger, V.2    Silani, V.3
  • 321
    • 33847787621 scopus 로고    scopus 로고
    • Therapeutic effects of immunization with mutant superoxide dismutase in mice models of amyotrophic lateral sclerosis
    • Urushitani, M.; Ezzi, S. A.; Julien, J. P. Therapeutic effects of immunization with mutant superoxide dismutase in mice models of amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. U. S. A. 2007, 104(7), 2495-2500.
    • (2007) Proc. Natl. Acad. Sci. U. S. A , vol.104 , Issue.7 , pp. 2495-2500
    • Urushitani, M.1    Ezzi, S.A.2    Julien, J.P.3
  • 322
    • 77951924183 scopus 로고    scopus 로고
    • Intracerebroventricular infusion of monoclonal antibody or its derived Fab fragment against misfolded forms of SOD1 mutant delays mortality in a mouse model of ALS
    • Gros-Louis, F.; Soucy, G.; Larivière, R.; Julien, J. P. Intracerebroventricular infusion of monoclonal antibody or its derived Fab fragment against misfolded forms of SOD1 mutant delays mortality in a mouse model of ALS. J. Neurochem., 2010, 113(5), 1188-1199.
    • (2010) J. Neurochem. , vol.113 , Issue.5 , pp. 1188-1199
    • Gros-Louis, F.1    Soucy, G.2    Larivière, R.3    Julien, J.P.4
  • 325
    • 79951664430 scopus 로고    scopus 로고
    • Inhibitors of advanced glycation and endoplasmic reticulum stress
    • Inagi, R. Inhibitors of advanced glycation and endoplasmic reticulum stress. Methods Enzymol. 2011, 491, 361-380.
    • (2011) Methods Enzymol , vol.491 , pp. 361-380
    • Inagi, R.1


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